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Transthyretin (ATTR) (Prealbumin) (TBPA)

 TTHY_HUMAN              Reviewed;         147 AA.
P02766; Q549C7; Q6IB96; Q9UBZ6; Q9UCM9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
27-SEP-2017, entry version 220.
RecName: Full=Transthyretin;
AltName: Full=ATTR;
AltName: Full=Prealbumin;
AltName: Full=TBPA;
Flags: Precursor;
Name=TTR; Synonyms=PALB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=6093805; DOI=10.1016/0006-291X(84)91590-0;
Mita S., Maeda S., Shimada K., Araki S.;
"Cloning and sequence analysis of cDNA for human prealbumin.";
Biochem. Biophys. Res. Commun. 124:558-564(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2990465; DOI=10.1016/0006-291X(85)91956-4;
Wallace M.R., Naylor S.L., Kluve-Beckerman B., Long G.L., McDonald L.,
Shows T.B., Benson M.D.;
"Localization of the human prealbumin gene to chromosome 18.";
Biochem. Biophys. Res. Commun. 129:753-758(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=4054629; DOI=10.1016/0378-1119(85)90272-0;
Sasaki H., Yoshioka N., Takagi Y., Sakaki Y.;
"Structure of the chromosomal gene for human serum prealbumin.";
Gene 37:191-197(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2995367;
Tsuzuki T., Mita S., Maeda S., Araki S., Shimada K.;
"Structure of the human prealbumin gene.";
J. Biol. Chem. 260:12224-12227(1985).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AMYL-TTR MET-50.
PubMed=3818577;
Mita S., Maeda S., Shimada K., Araki S.;
"Analyses of prealbumin mRNAs in individuals with familial amyloidotic
polyneuropathy.";
J. Biochem. 100:1215-1222(1986).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT AMYL-TTR MET-50.
TISSUE=Liver;
PubMed=3022108;
Maeda S., Mita S., Araki S., Shimada K.;
"Structure and expression of the mutant prealbumin gene associated
with familial amyloidotic polyneuropathy.";
Mol. Biol. Med. 3:329-338(1986).
[7]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-28.
TISSUE=Liver;
PubMed=2015890; DOI=10.1016/0014-5793(91)80387-I;
Christmanson L., Betsholtz C., Gustavsson A., Johansson B.,
Sletten K., Westermark P.;
"The transthyretin cDNA sequence is normal in transthyretin-derived
senile systemic amyloidosis.";
FEBS Lett. 281:177-180(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1666289;
Gu J.R., Jiang H.Q., He L.P., Li D.Z., Zhou X.M., Dai W.L., Qian L.F.,
Chen Y.Q., Schweinfest C., Papas T.;
"Transthyretin (prealbumin) gene in human primary hepatic cancer.";
Sci. China, Ser. B, Chem. Life Sci. Earth Sci. 34:1312-1318(1991).
[9]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
TISSUE=Retina;
PubMed=10328977; DOI=10.1006/exer.1998.0646;
Getz R.K., Kennedy B.G., Mangini N.J.;
"Transthyretin localization in cultured and native human retinal
pigment epithelium.";
Exp. Eye Res. 68:629-636(1999).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Corpus callosum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[15]
PROTEIN SEQUENCE OF 21-147.
PubMed=4607556;
Kanda Y., Goodman D.S., Canfield R.E., Morgan F.J.;
"The amino acid sequence of human plasma prealbumin.";
J. Biol. Chem. 249:6796-6805(1974).
[16]
PRELIMINARY PROTEIN SEQUENCE OF 21-147, AND VARIANT SER-26.
PubMed=6300852; DOI=10.1073/pnas.80.2.539;
Pras M., Prelli F., Franklin E.C., Frangione B.;
"Primary structure of an amyloid prealbumin variant in familial
polyneuropathy of Jewish origin.";
Proc. Natl. Acad. Sci. U.S.A. 80:539-542(1983).
[17]
PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR MET-50.
PubMed=6651852; DOI=10.1016/S0006-291X(83)80224-1;
Tawara S., Nakazato M., Kangawa K., Matsuo H., Araki S.;
"Identification of amyloid prealbumin variant in familial amyloidotic
polyneuropathy (Japanese type).";
Biochem. Biophys. Res. Commun. 116:880-888(1983).
[18]
PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR MET-50.
PubMed=6583672; DOI=10.1073/pnas.81.3.694;
Dwulet F.E., Benson M.D.;
"Primary structure of an amyloid prealbumin and its plasma precursor
in a heredofamilial polyneuropathy of Swedish origin.";
Proc. Natl. Acad. Sci. U.S.A. 81:694-698(1984).
[19]
PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR ILE-142.
PubMed=3135807; DOI=10.1016/0006-291X(88)90188-X;
Cornwell G.G. III, Sletten K., Johansson B., Westermark P.;
"Evidence that the amyloid fibril protein in senile systemic
amyloidosis is derived from normal prealbumin.";
Biochem. Biophys. Res. Commun. 154:648-653(1988).
[20]
PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR MET-50.
PubMed=1517749; DOI=10.1016/0022-510X(92)90048-P;
Kametani F., Ikeda S., Yanagisawa N., Ishi T., Hanyu N.;
"Characterization of a transthyretin-related amyloid fibril protein
from cerebral amyloid angiopathy in type I familial amyloid
polyneuropathy.";
J. Neurol. Sci. 108:178-183(1992).
[21]
PROTEIN SEQUENCE OF 21-41.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[22]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, AND VARIANT AMYL-TTR
LEU-53.
PubMed=1932142; DOI=10.1016/0925-4439(91)90033-6;
Harding J., Skare J., Skinner M.;
"A second transthyretin mutation at position 33 (Leu/Phe) associated
with familial amyloidotic polyneuropathy.";
Biochim. Biophys. Acta 1097:183-186(1991).
[23]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, VARIANT AMYL-TTR GLY-62,
AND VARIANT ASN-110.
PubMed=7923855;
Skare J.C., Jones L.A., Myles N., Kane K., Milunsky A., Cohen A.S.,
Skinner M.;
"Two transthyretin mutations (Glu42Gly, His90Asn) in an Italian family
with amyloidosis.";
Clin. Genet. 45:281-284(1994).
[24]
NUCLEOTIDE SEQUENCE [MRNA] OF 31-147.
PubMed=4044580;
Soprano D.R., Herbert J., Soprano K.J., Schon E.A., Goodman D.S.;
"Demonstration of transthyretin mRNA in the brain and other
extrahepatic tissues in the rat.";
J. Biol. Chem. 260:11793-11798(1985).
[25]
PROTEIN SEQUENCE OF 42-68; 101-123 AND 125-146, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[26]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-129, AND VARIANT DTTRH
THR-129.
PubMed=1979335; DOI=10.1172/JCI114938;
Moses A.C., Rosen H.N., Moller D.E., Tsuzaki S., Haddow J.E.,
Lawlor J., Liepnieks J.J., Nichols W.C., Benson M.D.;
"A point mutation in transthyretin increases affinity for thyroxine
and produces euthyroid hyperthyroxinemia.";
J. Clin. Invest. 86:2025-2033(1990).
[27]
PARTIAL PROTEIN SEQUENCE.
PubMed=7474944;
Gustavsson A., Jahr H., Tobiassen R., Jacobson D.R., Sletten K.,
Westermark P.;
"Amyloid fibril composition and transthyretin gene structure in senile
systemic amyloidosis.";
Lab. Invest. 73:703-708(1995).
[28]
BINDING SITES FOR THYROID HORMONES.
PubMed=201845; DOI=10.1038/268115a0;
Blake C.C.F., Oatley S.J.;
"Protein-DNA and protein-hormone interactions in prealbumin: a model
of the thyroid hormone nuclear receptor?";
Nature 268:115-120(1977).
[29]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=3714052; DOI=10.1212/WNL.36.7.900;
Herbert J., Wilcox J.N., Pham K.T., Fremeau R.T. Jr., Zeviani M.,
Dwork A., Soprano D.R., Makover A., Goodman D.S., Zimmerman E.A.,
Roberts J.L., Schon E.A.;
"Transthyretin: a choroid plexus-specific transport protein in human
brain. The 1986 S. Weir Mitchell award.";
Neurology 36:900-911(1986).
[30]
GLYCOSYLATION [LARGE SCALE ANALYSIS].
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[32]
GAMMA-CARBOXYGLUTAMATION AT GLU-62, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Cerebrospinal fluid;
PubMed=18221012; DOI=10.2174/092986608783330297;
Rueggeberg S., Horn P., Li X., Vajkoczy P., Franz T.;
"Detection of a gamma-carboxy-glutamate as novel post-translational
modification of human transthyretin.";
Protein Pept. Lett. 15:43-46(2008).
[33]
GLYCOSYLATION AT ASN-118, AND CHARACTERIZATION OF VARIANT AMYL-TTR
GLY-38.
PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
Ruiz-Canada C., Kelleher D.J., Gilmore R.;
"Cotranslational and posttranslational N-glycosylation of polypeptides
by distinct mammalian OST isoforms.";
Cell 136:272-283(2009).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=4216640; DOI=10.1016/0022-2836(74)90291-5;
Blake C.C.F., Geisow M.J., Swan I.D.A., Rerat C., Rerat B.;
"Structure of human plasma prealbumin at 2.5-A resolution. A
preliminary report on the polypeptide chain conformation, quaternary
structure and thyroxine binding.";
J. Mol. Biol. 88:1-12(1974).
[36]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=671542; DOI=10.1016/0022-2836(78)90368-6;
Blake C.C.F., Geisow M.J., Oatley S.J., Rerat B., Rerat C.;
"Structure of prealbumin: secondary, tertiary and quaternary
interactions determined by Fourier refinement at 1.8 A.";
J. Mol. Biol. 121:339-356(1978).
[37]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
PubMed=8382610;
Terry C.J., Damas A.M., Oliveira P., Saraiva M.J.M., Alves I.L.,
Costa P.P., Matias P.M., Sakaki Y., Blake C.C.F.;
"Structure of Met30 variant of transthyretin and its amyloidogenic
implications.";
EMBO J. 12:735-741(1993).
[38]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
PubMed=8428915;
Hamilton J.A., Steinrauf L.K., Braden B.C., Liepnieks J., Benson M.D.,
Holmgren G., Sandgren O., Steen L.;
"The X-ray crystal structure refinements of normal human transthyretin
and the amyloidogenic Val-30-->Met variant to 1.7-A resolution.";
J. Biol. Chem. 268:2416-2424(1993).
[39]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH RBP.
PubMed=7754382; DOI=10.1126/science.7754382;
Monaco H.L., Rizzi M., Coda A.;
"Structure of a complex of two plasma proteins: transthyretin and
retinol-binding protein.";
Science 268:1039-1041(1995).
[40]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANTS.
PubMed=9818054; DOI=10.3109/13506129809003843;
Schormann N., Murrell J.R., Benson M.D.;
"Tertiary structures of amyloidogenic and non-amyloidogenic
transthyretin variants: new model for amyloid fibril formation.";
Amyloid 5:175-187(1998).
[41]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR
PRO-75.
PubMed=9733771; DOI=10.1074/jbc.273.38.24715;
Sebastiao M.P., Saraiva M.J., Damas A.M.;
"The crystal structure of amyloidogenic Leu55 --> Pro transthyretin
variant reveals a possible pathway for transthyretin polymerization
into amyloid fibrils.";
J. Biol. Chem. 273:24715-24722(1998).
[42]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=9789022; DOI=10.1073/pnas.95.22.12956;
Peterson S.A., Klabunde T., Lashuel H.A., Purkey H., Sacchettini J.C.,
Kelly J.W.;
"Inhibiting transthyretin conformational changes that lead to amyloid
fibril formation.";
Proc. Natl. Acad. Sci. U.S.A. 95:12956-12960(1998).
[43]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH RBP4, AND
SUBUNIT.
PubMed=10052934; DOI=10.1021/bi982291i;
Naylor H.M., Newcomer M.E.;
"The structure of human retinol-binding protein (RBP) with its carrier
protein transthyretin reveals an interaction with the carboxy terminus
of RBP.";
Biochemistry 38:2647-2653(1999).
[44]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147.
PubMed=10986125; DOI=10.1006/jmbi.2000.4078;
Hoernberg A., Eneqvist T., Olofsson A., Lundgren E.,
Sauer-Eriksson A.E.;
"A comparative analysis of 23 structures of the amyloidogenic protein
transthyretin.";
J. Mol. Biol. 302:649-669(2000).
[45]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=10742177; DOI=10.1038/74082;
Klabunde T., Petrassi H.M., Oza V.B., Raman P., Kelly J.W.,
Sacchettini J.C.;
"Rational design of potent human transthyretin amyloid disease
inhibitors.";
Nat. Struct. Biol. 7:312-321(2000).
[46]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-147, MUTAGENESIS OF
PHE-107 AND LEU-130, IDENTIFICATION BY MASS SPECTROMETRY, FORMATION OF
AMYLOID FIBERS AT ACIDIC PH, AND SUBUNIT.
PubMed=11560492; DOI=10.1021/bi011194d;
Jiang X., Smith C.S., Petrassi H.M., Hammarstroem P., White J.T.,
Sacchettini J.C., Kelly J.W.;
"An engineered transthyretin monomer that is nonamyloidogenic, unless
it is partially denatured.";
Biochemistry 40:11442-11452(2001).
[47]
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 30-144 OF VARIANT AMYL-TTR
MET-50 AND VARIANT CHICAGO MET-139 IN COMPLEX WITH L-THYROXINE, AND
SUBUNIT.
PubMed=11243784; DOI=10.1006/jmbi.2000.4415;
Sebastiao M.P., Lamzin V., Saraiva M.J., Damas A.M.;
"Transthyretin stability as a key factor in amyloidogenesis: X-ray
analysis at atomic resolution.";
J. Mol. Biol. 306:733-744(2001).
[48]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR
CYS-134.
PubMed=12403615; DOI=10.1021/bi025800w;
Eneqvist T., Olofsson A., Ando Y., Miyakawa T., Katsuragi S., Jass J.,
Lundgren E., Sauer-Eriksson A.E.;
"Disulfide-bond formation in the transthyretin mutant Y114C prevents
amyloid fibril formation in vivo and in vitro.";
Biochemistry 41:13143-13151(2002).
[49]
X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147IN COMPLEX WITH
AMYLOIDOGENESIS INHIBITORS.
PubMed=12820260; DOI=10.1002/anie.200351179;
Razavi H., Palaninathan S.K., Powers E.T., Wiseman R.L., Purkey H.E.,
Mohamedmohaideen N.N., Deechongkit S., Chiang K.P., Dendle M.T.A.,
Sacchettini J.C., Kelly J.W.;
"Benzoxazoles as transthyretin amyloid fibril inhibitors: synthesis,
evaluation, and mechanism of action.";
Angew. Chem. Int. Ed. 42:2758-2761(2003).
[50]
X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 21-147 IN COMPLEX WITH
AMYLOIDOGENESIS INHIBITORS, AND FIBRIL FORMATION.
PubMed=14583036; DOI=10.1021/ja030294z;
Green N.S., Palaninathan S.K., Sacchettini J.C., Kelly J.W.;
"Synthesis and characterization of potent bivalent amyloidosis
inhibitors that bind prior to transthyretin tetramerization.";
J. Am. Chem. Soc. 125:13404-13414(2003).
[51]
X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147 IN COMPLEX WITH
DIFLUNISAL ANALOGS, AND INHIBITION OF AMYLOID FORMATION.
PubMed=14711308; DOI=10.1021/jm030347n;
Adamski-Werner S.L., Palaninathan S.K., Sacchettini J.C., Kelly J.W.;
"Diflunisal analogues stabilize the native state of transthyretin.
Potent inhibition of amyloidogenesis.";
J. Med. Chem. 47:355-374(2004).
[52]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR
PHE-98 AND VARIANT HIS-124, AND SUBUNIT.
PubMed=15735344; DOI=10.1107/S0907444904034316;
Neto-Silva R.M., Macedo-Ribeiro S., Pereira P.J.B., Coll M.,
Saraiva M.J., Damas A.M.;
"X-ray crystallographic studies of two transthyretin variants: further
insights into amyloidogenesis.";
Acta Crystallogr. D 61:333-339(2005).
[53]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147 IN COMPLEXES WITH
CHLORIDE AND IODIDE IONS.
PubMed=15981995; DOI=10.1021/bi050249z;
Hoernberg A., Hultdin U.W., Olofsson A., Sauer-Eriksson A.E.;
"The effect of iodide and chloride on transthyretin structure and
stability.";
Biochemistry 44:9290-9299(2005).
[54]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR
CYS-134.
PubMed=16185074; DOI=10.1021/bi050795s;
Karlsson A., Olofsson A., Eneqvist T., Sauer-Eriksson A.E.;
"Cys114-linked dimers of transthyretin are compatible with amyloid
formation.";
Biochemistry 44:13063-13070(2005).
[55]
X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 21-147 IN COMPLEX WITH
THYROID HORMONE ANALOG, AND SUBUNIT.
PubMed=15826192; DOI=10.1021/ja042929f;
Wiseman R.L., Johnson S.M., Kelker M.S., Foss T., Wilson I.A.,
Kelly J.W.;
"Kinetic stabilization of an oligomeric protein by a single ligand
binding event.";
J. Am. Chem. Soc. 127:5540-5551(2005).
[56]
X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 31-147, AND SUBUNIT.
PubMed=15769474; DOI=10.1016/j.jmb.2005.01.050;
Foss T.R., Kelker M.S., Wiseman R.L., Wilson I.A., Kelly J.W.;
"Kinetic stabilization of the native state by protein engineering:
implications for inhibition of transthyretin amyloidogenesis.";
J. Mol. Biol. 347:841-854(2005).
[57]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF WILD-TYPE AND
VARIANTS AMYL-TTR PRO-75 AND PHE-98.
PubMed=16627944; DOI=10.1107/S0907444906006962;
Morais-de-Sa E., Neto-Silva R.M., Pereira P.J.B., Saraiva M.J.,
Damas A.M.;
"The binding of 2,4-dinitrophenol to wild-type and amyloidogenic
transthyretin.";
Acta Crystallogr. D 62:512-519(2006).
[58]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 21-147.
PubMed=17175208; DOI=10.1016/j.bbapap.2006.10.015;
Gales L., Saraiva M.J., Damas A.M.;
"Structural basis for the protective role of sulfite against
transthyretin amyloid formation.";
Biochim. Biophys. Acta 1774:59-64(2007).
[59]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147.
PubMed=17196219; DOI=10.1016/j.jmb.2006.11.076;
Pasquato N., Berni R., Folli C., Alfieri B., Cendron L., Zanotti G.;
"Acidic pH-induced conformational changes in amyloidogenic mutant
transthyretin.";
J. Mol. Biol. 366:711-719(2007).
[60]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 IN COMPLEX WITH
3,5-DIIODOSALICYLIC ACID, AND THYROXINE BINDING.
PubMed=18155178; DOI=10.1016/j.bbapap.2007.11.014;
Gales L., Almeida M.R., Arsequell G., Valencia G., Saraiva M.J.,
Damas A.M.;
"Iodination of salicylic acid improves its binding to transthyretin.";
Biochim. Biophys. Acta 1784:512-517(2008).
[61]
X-RAY CRYSTALLOGRAPHY (3.38 ANGSTROMS) OF 21-147 IN COMPLEX WITH RBP4.
PubMed=19021760; DOI=10.1111/j.1742-4658.2008.06705.x;
Zanotti G., Folli C., Cendron L., Alfieri B., Nishida S.K.,
Gliubich F., Pasquato N., Negro A., Berni R.;
"Structural and mutational analyses of protein-protein interactions
between transthyretin and retinol-binding protein.";
FEBS J. 275:5841-5854(2008).
[62]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147 IN COMPLEX WITH
2-ARYLBENZOXAZOLE-BASED TRANSTHYRETIN AMYLOIDOGENESIS INHIBITORS.
PubMed=18095641; DOI=10.1021/jm0708735;
Johnson S.M., Connelly S., Wilson I.A., Kelly J.W.;
"Biochemical and structural evaluation of highly selective 2-
arylbenzoxazole-based transthyretin amyloidogenesis inhibitors.";
J. Med. Chem. 51:260-270(2008).
[63]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 21-147 IN COMPLEX WITH
BISARYL AMYLOIDOGENESIS INHIBITORS.
PubMed=18811132; DOI=10.1021/jm800435s;
Johnson S.M., Connelly S., Wilson I.A., Kelly J.W.;
"Toward optimization of the linker substructure common to
transthyretin amyloidogenesis inhibitors using biochemical and
structural studies.";
J. Med. Chem. 51:6348-6358(2008).
[64]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 21-147 AT PH 3.5 AND 4.5.
PubMed=18662699; DOI=10.1016/j.jmb.2008.07.029;
Palaninathan S.K., Mohamedmohaideen N.N., Snee W.C., Kelly J.W.,
Sacchettini J.C.;
"Structural insight into pH-induced conformational changes within the
native human transthyretin tetramer.";
J. Mol. Biol. 382:1157-1167(2008).
[65]
X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 21-147.
Mycobacterium tuberculosis structural genomics consortium (TB);
"Crystal structure of the F87M/L110M mutant of human transthyretin at
pH 4.6 soaked.";
Submitted (JUL-2008) to the PDB data bank.
[66]
REVIEW ON VARIANTS.
PubMed=7599630; DOI=10.1002/humu.1380050302;
Saraiva M.J.M.;
"Transthyretin mutations in health and disease.";
Hum. Mutat. 5:191-196(1995).
[67]
VARIANT AMYL-TTR ILE-53.
PubMed=6487335; DOI=10.1016/S0006-291X(84)80222-3;
Nakazato M., Kangawa K., Minamino N., Tawara S., Matsuo H., Araki S.;
"Revised analysis of amino acid replacement in a prealbumin variant
(SKO-III) associated with familial amyloidotic polyneuropathy of
Jewish origin.";
Biochem. Biophys. Res. Commun. 123:921-928(1984).
[68]
VARIANT AMYL-TTR SER-104.
PubMed=3722385; DOI=10.1172/JCI112573;
Wallace M.R., Dwulet F.E., Conneally P.M., Benson M.D.;
"Biochemical and molecular genetic characterization of a new variant
prealbumin associated with hereditary amyloidosis.";
J. Clin. Invest. 78:6-12(1986).
[69]
VARIANT VAL-136.
PubMed=3675594; DOI=10.1016/0006-291X(87)91135-1;
Strahler J.R., Rosenblum B.B., Hanash S.M.;
"Identification and characterization of a human transthyretin
variant.";
Biochem. Biophys. Res. Commun. 148:471-477(1987).
[70]
VARIANT AMYL-TTR TYR-97.
PubMed=2891727; DOI=10.1172/JCI113293;
Wallace M.R., Dwulet F.E., Williams E.C., Conneally P.M., Benson M.D.;
"Identification of a new hereditary amyloidosis prealbumin variant,
Tyr-77, and detection of the gene by DNA analysis.";
J. Clin. Invest. 81:189-193(1988).
[71]
VARIANT AMYL-TTR CYS-134.
PubMed=2161654; DOI=10.1016/0006-291X(90)91445-X;
Ueno S., Uemichi T., Yorifuji S., Tarui S.;
"A novel variant of transthyretin (Tyr114 to Cys) deduced from the
nucleotide sequences of gene fragments from familial amyloidotic
polyneuropathy in Japanese sibling cases.";
Biochem. Biophys. Res. Commun. 169:143-147(1990).
[72]
VARIANTS AMYL-TTR GLY-62 AND ARG-70.
PubMed=2363717; DOI=10.1016/0006-291X(90)92011-N;
Ueno S., Uemichi T., Takahashi N., Soga F., Yorifuji S., Tarui S.;
"Two novel variants of transthyretin identified in Japanese cases with
familial amyloidotic polyneuropathy: transthyretin (Glu42 to Gly) and
transthyretin (Ser50 to Arg).";
Biochem. Biophys. Res. Commun. 169:1117-1121(1990).
[73]
VARIANT CHICAGO MET-139.
PubMed=1877623; DOI=10.1002/ajmg.1320390415;
Harrison H.H., Gordon E.D., Nichols W.C., Benson M.D.;
"Biochemical and clinical characterization of prealbuminCHICAGO: an
apparently benign variant of serum prealbumin (transthyretin)
discovered with high-resolution two-dimensional electrophoresis.";
Am. J. Med. Genet. 39:442-452(1991).
[74]
VARIANT AMYL-TTR ARG-78.
PubMed=1656975; DOI=10.1016/S0006-291X(05)81304-X;
Saeki Y., Ueno S., Yorifuji S., Sugiyama Y., Ide Y., Matsuzawa Y.;
"New mutant gene (transthyretin Arg 58) in cases with hereditary
polyneuropathy detected by non-isotope method of single-strand
conformation polymorphism analysis.";
Biochem. Biophys. Res. Commun. 180:380-385(1991).
[75]
VARIANT ASN-110.
PubMed=1997217;
Skare J.C., Milunsky J.M., Milunsky A., Skare I.B., Cohen A.S.,
Skinner M.;
"A new transthyretin variant from a patient with familial amyloidotic
polyneuropathy has asparagine substituted for histidine at position
90.";
Clin. Genet. 39:6-12(1991).
[76]
VARIANTS AMYL-TTR LEU-53 AND LEU-84.
PubMed=2046936; DOI=10.1212/WNL.41.6.893;
Li S., Minnerath S., Li K., Dyck P.J., Sommer S.S.;
"Two-tiered DNA-based diagnosis of transthyretin amyloidosis reveals
two novel point mutations.";
Neurology 41:893-898(1991).
[77]
VARIANT AMYL-TTR THR-65.
PubMed=1570831;
Saraiva M.J.M., Almeida M.R., Sherman W., Gawinowicz M., Costa P.,
Costa P.P., Goodman D.S.;
"A new transthyretin mutation associated with amyloid
cardiomyopathy.";
Am. J. Hum. Genet. 50:1027-1030(1992).
[78]
VARIANT AMYL-TTR ARG-67.
PubMed=1734866; DOI=10.1016/0006-291X(92)91763-G;
Murakami T., Maeda S., Yi S., Ikegawa S., Kawashima E., Onodera S.,
Shimada K., Araki S.;
"A novel transthyretin mutation associated with familial amyloidotic
polyneuropathy.";
Biochem. Biophys. Res. Commun. 182:520-526(1992).
[79]
VARIANT AMYL-TTR LEU-50.
PubMed=1520326; DOI=10.1016/S0006-291X(05)81506-2;
Murakami T., Atsumi T., Maeda S., Tanase S., Ishikawa K., Mita S.,
Kumamoto T., Araki S., Ando M.;
"A novel transthyretin mutation at position 30 (Leu for Val)
associated with familial amyloidotic polyneuropathy.";
Biochem. Biophys. Res. Commun. 187:397-403(1992).
[80]
VARIANT AMYL-TTR ILE-70.
PubMed=1520336; DOI=10.1016/S0006-291X(05)81516-5;
Nishi H., Kimura A., Harada H., Hayashi Y., Nakamura M., Sasazuki T.;
"Novel variant transthyretin gene (Ser50 to Ile) in familial cardiac
amyloidosis.";
Biochem. Biophys. Res. Commun. 187:460-466(1992).
[81]
VARIANT AMYL-TTR ALA-50.
PubMed=1544214;
Jones L.A., Skare J.C., Cohen A.S., Harding J.A., Milunsky A.,
Skinner M.;
"Familial amyloidotic polyneuropathy: a new transthyretin position 30
mutation (alanine for valine) in a family of German descent.";
Clin. Genet. 41:70-73(1992).
[82]
VARIANT AMYL-TTR PRO-75.
PubMed=1351039; DOI=10.1007/BF00220559;
Jacobson D.R., McFarlin D.E., Kane I., Buxbaum J.N.;
"Transthyretin Pro55, a variant associated with early-onset,
aggressive, diffuse amyloidosis with cardiac and neurologic
involvement.";
Hum. Genet. 89:353-356(1992).
[83]
VARIANTS AMYL-TTR ALA-69 AND GLN-109.
PubMed=1301926; DOI=10.1002/humu.1380010306;
Almeida M.R., Ferlini A., Forabosco A., Gawinowicz M.A., Costa P.P.,
Salvi F., Plasmati R., Tassinari C.A., Altland K., Saraiva M.J.;
"Two transthyretin variants (TTR Ala-49 and TTR Gln-89) in two
Sicilian kindreds with hereditary amyloidosis.";
Hum. Mutat. 1:211-215(1992).
[84]
VARIANT AMYL-TTR ARG-30.
PubMed=1362222; DOI=10.1136/jmg.29.12.888;
Uemichi T., Murrel J.R., Zeldenrust S., Benson M.D.;
"A new mutant transthyretin (Arg 10) associated with familial amyloid
polyneuropathy.";
J. Med. Genet. 29:888-891(1992).
[85]
VARIANT AMYL-TTR ASN-90.
PubMed=1436517; DOI=10.1212/WNL.42.11.2094;
Izumoto S., Younger D., Hays A.P., Martone R.L., Smith R.T.,
Herbert J.;
"Familial amyloidotic polyneuropathy presenting with carpal tunnel
syndrome and a new transthyretin mutation, asparagine 70.";
Neurology 42:2094-2102(1992).
[86]
VARIANT AMYL-TTR LYS-81.
PubMed=8352764; DOI=10.1006/bbrc.1993.1933;
Shiomi K., Nakazato M., Matsukura S., Ohnishi A., Hatanaka H.,
Tsuji S., Murai Y., Kojima M., Kangawa K., Matsuo H.;
"A basic transthyretin variant (Glu61-->Lys) causes familial
amyloidotic polyneuropathy: protein and DNA sequencing and PCR-induced
mutation restriction analysis.";
Biochem. Biophys. Res. Commun. 194:1090-1096(1993).
[87]
VARIANT AMYL-TTR LEU-88.
PubMed=8038017; DOI=10.1136/hrt.70.2.111;
Hesse A., Altland K., Linke R.P., Almeida M.R., Saraiva M.J.M.,
Steinmetz A., Maisch B.;
"Cardiac amyloidosis: a review and report of a new transthyretin
(prealbumin) variant.";
Br. Heart J. 70:111-115(1993).
[88]
VARIANT AMYL-TTR ALA-91.
PubMed=8257997; DOI=10.1002/humu.1380020516;
Almeida M.R., Lopez-Andreu F., Munar-Ques M., Costa P.P.,
Saraiva M.J.;
"Transthyretin Ala-71: a new transthyretin variant in a Spanish family
with familial amyloidotic polyneuropathy.";
Hum. Mutat. 2:420-421(1993).
[89]
VARIANT AMYL-TTR ALA-91.
PubMed=8095302; DOI=10.1136/jmg.30.2.120;
Benson M.D. II, Turpin J.C., Lucotte G., Zeldenrust S.,
Lechevalier B., Benson M.D.;
"A transthyretin variant (alanine 71) associated with familial
amyloidotic polyneuropathy in a French family.";
J. Med. Genet. 30:120-122(1993).
[90]
VARIANT AMYL-TTR ALA-67.
Ferlini A., Salvi F., Patrosso C., Fini S., Vezzoni P., Forbasco A.;
"Gly47Ala: a new transthyretin gene mutation in hereditary amyloidosis
TTR-related.";
J. Rheumatol. 20:187-187(1993).
[91]
VARIANT SER-26, AND VARIANT AMYL-TTR ILE-53.
PubMed=8019560; DOI=10.1002/humu.1380030313;
Jacobson D.R., Buxbaum J.N.;
"A double-variant transthyretin allele (Ser 6, Ile 33) in the Israeli
patient 'SKO' with familial amyloidotic polyneuropathy.";
Hum. Mutat. 3:254-260(1994).
[92]
VARIANT AMYL-TTR VAL-127.
PubMed=8081397; DOI=10.1002/humu.1380030414;
Jacobson D., Gertz M.A., Buxbaum J.N.;
"Transthyretin VAL107, a new variant associated with familial cardiac
and neuropathic amyloidosis.";
Hum. Mutat. 3:399-401(1994).
[93]
VARIANT SER-104, AND RBP BINDING STUDIES.
PubMed=8089102;
Berni R., Malpeli G., Folli C., Murrell J.R., Liepnieks J.J.,
Benson M.D.;
"The Ile-84-->Ser amino acid substitution in transthyretin interferes
with the interaction with plasma retinol-binding protein.";
J. Biol. Chem. 269:23395-23398(1994).
[94]
VARIANT AMYL-TTR VAL-127.
PubMed=7914929; DOI=10.1136/jmg.31.5.416;
Uemichi T., Gertz M.A., Benson M.D.;
"Amyloid polyneuropathy in two German-American families: a new
transthyretin variant (Val 107).";
J. Med. Genet. 31:416-417(1994).
[95]
VARIANT AMYL-TTR GLY-117.
PubMed=8133316; DOI=10.1016/0022-510X(94)90162-7;
Yasuda T., Sobue G., Doyu M., Nakazato M., Shiomi K., Yanagi T.,
Mitsuma T.;
"Familial amyloidotic polyneuropathy with late-onset and well-
preserved autonomic function: a Japanese kindred with novel mutant
transthyretin (Ala97 to Gly).";
J. Neurol. Sci. 121:97-102(1994).
[96]
VARIANT AMYL-TTR PRO-75.
PubMed=7910950; DOI=10.1002/mus.880170611;
Yamamoto K., Hsu S.P., Yoshida K., Ikeda S., Nakazato M., Shiomi K.,
Cheng S.Y., Furihata K., Ueno I., Yanagisawa N.;
"Familial amyloid polyneuropathy in Taiwan: identification of
transthyretin variant (Leu55-->Pro).";
Muscle Nerve 17:637-641(1994).
[97]
VARIANT CTS1 HIS-134.
PubMed=8309582; DOI=10.1212/WNL.44.2.315;
Murakami T., Tachibana S., Endo Y., Kawai R., Hara M., Tanase S.,
Ando M.;
"Familial carpal tunnel syndrome due to amyloidogenic transthyretin
His 114 variant.";
Neurology 44:315-318(1994).
[98]
VARIANTS AMYL-TTR MET-50; ASN-55; ALA-69; ARG-70; ALA-80; TYR-97 AND
GLN-109.
PubMed=7655883; DOI=10.1093/brain/118.4.849;
Reilly M.M., Adams D., Booth D.R., Davis M.B., Said G.,
Laubriat-Bianchin M., Pepys M.B., Thomas P.K., Harding A.E.;
"Transthyretin gene analysis in European patients with suspected
familial amyloid polyneuropathy.";
Brain 118:849-856(1995).
[99]
VARIANT AMYL-TTR LYS-79.
PubMed=7850982; DOI=10.1161/01.CIR.91.4.962;
Booth D.R., Tan S.Y., Hawkins P.N., Pepys M.B., Frustaci A.;
"A novel variant of transthyretin, 59Thr-->Lys, associated with
autosomal dominant cardiac amyloidosis in an Italian family.";
Circulation 91:962-967(1995).
[100]
VARIANT AMYL-TTR GLY-38.
PubMed=8579098;
Vidal R., Garzuly F., Budka H., Lalowski M., Linke R.P., Brittig F.,
Frangione B., Wisniewski T.;
"Meningocerebrovascular amyloidosis associated with a novel
transthyretin mis-sense mutation at codon 18 (TTRD 18G).";
Am. J. Pathol. 148:361-366(1996).
[101]
VARIANT AMYL-TTR GLY-50.
PubMed=9066351; DOI=10.1002/ana.410410305;
Petersen R.B., Goren H., Cohen M., Richardson S.L., Tresser N.,
Lynn A., Gali M., Estes M., Gambetti P.;
"Transthyretin amyloidosis: a new mutation associated with dementia.";
Ann. Neurol. 41:307-313(1997).
[102]
VARIANT AMYL-TTR ILE-40.
PubMed=8990019;
DOI=10.1002/(SICI)1098-1004(1997)9:1<83::AID-HUMU19>3.0.CO;2-L;
Jacobson D.R., Pan T., Kyle R.A., Buxbaum J.N.;
"Transthyretin ILE20, a new variant associated with late-onset cardiac
amyloidosis.";
Hum. Mutat. 9:83-85(1997).
[103]
VARIANT AMYL-TTR THR-54.
PubMed=9605286;
DOI=10.1002/(SICI)1096-8628(19980501)77:2<135::AID-AJMG5>3.0.CO;2-R;
Patrosso M.C., Salvi F., De Grandis D., Vezzoni P., Jacobson D.R.,
Ferlini A.;
"Novel transthyretin missense mutation (Thr34) in an Italian family
with hereditary amyloidosis.";
Am. J. Med. Genet. 77:135-138(1998).
[104]
VARIANT AMYL-TTR ASP-62.
PubMed=10036587; DOI=10.3109/13506129809007302;
Dupuy O., Bletry O., Blanc A.S., Droz D., Viemont M., Delpech M.,
Grateau G.;
"A novel variant of transthyretin (Glu42Asp) associated with sporadic
late-onset cardiac amyloidosis.";
Amyloid 5:285-287(1998).
[105]
VARIANTS AMYL-TTR SER-111 AND SER-136.
PubMed=10627135;
DOI=10.1002/(SICI)1098-1004(1998)12:1<71::AID-HUMU15>3.0.CO;2-7;
Misrahi A.M., Plante V., Lalu T., Serre I., Adams D., Lacroix D.C.,
Said G.;
"New transthyretin variants Ser 91 and Ser 116 associated with
familial amyloidotic polyneuropathy.";
Hum. Mutat. 12:71-71(1998).
[106]
VARIANT AMYL-TTR VAL-93.
PubMed=10694917;
DOI=10.1002/(SICI)1098-1004(1998)12:2<135::AID-HUMU9>3.0.CO;2-K;
Booth D.R., Gillmore J.D., Persey M.R., Booth S.E., Cafferty K.D.,
Tennent G.A., Madhoo S., Cochrane S.W., Whitehead T.C., Pasvol G.,
Hawkins P.N.;
"Transthyretin Ile73Val is associated with familial amyloidotic
polyneuropathy in a Bangladeshi family.";
Hum. Mutat. 12:135-135(1998).
[107]
VARIANT SER-121, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10671063;
Kishikawa M., Nakanishi T., Miyazaki A., Hatanaka M., Shimizu A.,
Tamoto S., Ohsawa N., Hayashi H., Kanai M.;
"A new nonamyloid transthyretin variant, G101S, detected by
electrospray ionization/mass spectrometry.";
Hum. Mutat. 12:363-363(1998).
[108]
VARIANT SER-64.
PubMed=9818883; DOI=10.1212/WNL.51.5.1462;
Klein C.J., Nakumura M., Jacobson D.R., Lacy M.Q., Benson M.D.,
Petersen R.C.;
"Transthyretin amyloidosis (serine 44) with headache, hearing loss,
and peripheral neuropathy.";
Neurology 51:1462-1464(1998).
[109]
VARIANT AMYL-TTR ALA-142, VARIANT SER-26, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=10211412; DOI=10.3109/13506129908993288;
Theberge R., Connors L., Skare J., Skinner M., Falk R.H.,
Costello C.E.;
"A new amyloidogenic transthyretin variant (Val122Ala) found in a
compound heterozygous patient.";
Amyloid 6:54-58(1999).
[110]
VARIANT AMYL-TTR ASN-43, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10439117; DOI=10.3109/13506129909007311;
Connors L.H., Theberge R., Skare J., Costello C.E., Falk R.H.,
Skinner M.;
"A new transthyretin variant (Ser23Asn) associated with familial
amyloidosis in a Portuguese patient.";
Amyloid 6:114-118(1999).
[111]
VARIANTS AMYL-TTR LEU-50; VAL-53; ALA-58; ARG-70; GLY-117 AND SER-117,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10611950; DOI=10.3109/13506129909007341;
Tachibana N., Tokuda T., Yoshida K., Taketomi T., Nakazato M.,
Li Y.F., Masuda Y., Ikeda S.;
"Usefulness of MALDI/TOF mass spectrometry of immunoprecipitated serum
variant transthyretin in the diagnosis of familial amyloid
polyneuropathy.";
Amyloid 6:282-288(1999).
[112]
VARIANT HIS-124, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10529370; DOI=10.1006/bbrc.1999.1514;
Terazaki H., Ando Y., Misumi S., Nakamura M., Ando E., Matsunaga N.,
Shoji S., Okuyama M., Ideta H., Nakagawa K., Ishizaki T., Ando M.,
Saraiva M.J.;
"A novel compound heterozygote (FAP ATTR Arg104His/ATTR Val30Met) with
high serum transthyretin (TTR) and retinol binding protein (RBP)
levels.";
Biochem. Biophys. Res. Commun. 264:365-370(1999).
[113]
VARIANT AMYL-TTR PRO-32.
PubMed=10071047; DOI=10.1093/brain/122.2.183;
Brett M., Persey M.R., Reilly M.M., Revesz T., Booth D.R., Booth S.E.,
Hawkins P.N., Pepys M.B., Morgan-Hughes J.A.;
"Transthyretin Leu12Pro is associated with systemic, neuropathic and
leptomeningeal amyloidosis.";
Brain 122:183-190(1999).
[114]
VARIANT AMYL-TTR ILE-69, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10436378; DOI=10.1159/000022872;
Nakamura M., Yamashita T., Ando Y., Hamidi Asl K., Tashima K.,
Ohlsson P., Kususe Y., Benson M.D.;
"Identification of a new transthyretin variant (Ile49) in familial
amyloidotic polyneuropathy using electrospray ionization mass
spectrometry and nonisotopic RNase cleavage assay.";
Hum. Hered. 49:186-189(1999).
[115]
VARIANT AMYL-TTR LYS-109.
PubMed=10842705; DOI=10.3109/13506120009146824;
Nakamura M., Hamidi Asl K., Benson M.D.;
"A novel variant of transthyretin (Glu89Lys) associated with familial
amyloidotic polyneuropathy.";
Amyloid 7:46-50(2000).
[116]
VARIANT AMYL-TTR SER-65, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10842718; DOI=10.3109/13506120009146252;
Janunger T., Anan I., Holmgren G., Lovheim O., Ohlsson P.I.,
Suhr O.B., Tashima K.;
"Heart failure caused by a novel amyloidogenic mutation of the
transthyretin gene: ATTR Ala45Ser.";
Amyloid 7:137-140(2000).
[117]
VARIANT AMYL-TTR MET-48.
PubMed=10882995;
DOI=10.1002/1097-4598(200007)23:7<1016::AID-MUS3>3.0.CO;2-W;
de Carvalho M., Moreira P., Evangelista T., Ducla-Soares J.L.,
Bento M., Fernandes R., Saraiva M.J.;
"New transthyretin mutation V28M in a Portuguese kindred with amyloid
polyneuropathy.";
Muscle Nerve 23:1016-1021(2000).
[118]
VARIANT AMYL-TTR GLU-73.
PubMed=11445644; DOI=10.1212/WNL.57.1.135;
Ellie E., Camou F., Vital A., Rummens C., Grateau G., Delpech M.,
Valleix S.;
"Recurrent subarachnoid hemorrhage associated with a new transthyretin
variant (Gly53Glu).";
Neurology 57:135-137(2001).
[119]
VARIANT AMYL-TTR GLN-75.
PubMed=12557757; DOI=10.3109/13506120209114105;
Yazaki M., Varga J., Dyck P.J., Benson M.D.;
"A new transthyretin variant Leu55Gln in a patient with systemic
amyloidosis.";
Amyloid 9:268-271(2002).
[120]
VARIANTS SER-26 AND MET-139, VARIANTS AMYL-TTR ALA-58; LEU-61; SER-64
AND LEU-84, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11866053; DOI=10.1021/ac010780+;
Lim A., Prokaeva T., McComb M.E., O'Connor P.B., Theberge R.,
Connors L.H., Skinner M., Costello C.E.;
"Characterization of transthyretin variants in familial transthyretin
amyloidosis by mass spectrometric peptide mapping and DNA sequence
analysis.";
Anal. Chem. 74:741-751(2002).
[121]
VARIANTS AMYL-TTR MET-50; LEU-53; VAL-53; VAL-58; GLU-67; ALA-80;
SER-140 AND ILE-142.
PubMed=12050338; DOI=10.1056/NEJMoa013354;
Lachmann H.J., Booth D.R., Booth S.E., Bybee A., Gilbertson J.A.,
Gillmore J.D., Pepys M.B., Hawkins P.N.;
"Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis.";
N. Engl. J. Med. 346:1786-1791(2002).
[122]
VARIANT AMYL-TTR HIS-89.
PubMed=12771253; DOI=10.1212/01.WNL.0000065901.18353.AB;
Blevins G., Macaulay R., Harder S., Fladeland D., Yamashita T.,
Yazaki M., Hamidi Asl K., Benson M.D., Donat J.R.;
"Oculoleptomeningeal amyloidosis in a large kindred with a new
transthyretin variant Tyr69His.";
Neurology 60:1625-1630(2003).
[123]
VARIANT CYS-53, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12876326; DOI=10.1110/ps.0349703;
Lim A., Prokaeva T., McComb M.E., Connors L.H., Skinner M.,
Costello C.E.;
"Identification of S-sulfonation and S-thiolation of a novel
transthyretin Phe33Cys variant from a patient diagnosed with familial
transthyretin amyloidosis.";
Protein Sci. 12:1775-1785(2003).
[124]
VARIANT AMYL-TTR LYS-74.
PubMed=15214015; DOI=10.1002/ajmg.a.30007;
Busse A., Sanchez M.A., Monterroso V., Alvarado M.V., Leon P.;
"A severe form of amyloidotic polyneuropathy in a Costa Rican family
with a rare transthyretin mutation (Glu54Lys).";
Am. J. Med. Genet. A 128:190-194(2004).
[125]
VARIANT AMYL-TTR VAL-53.
PubMed=15478468; DOI=10.1080/13506120410001727767;
Frigerio R., Fabrizi G.M., Ferrarini M., Cavallaro T., Brighina L.,
Santoro P., Agostoni E., Cavaletti G., Rizzuto N., Ferrarese C.;
"An unusual transthyretin gene missense mutation (TTR Phe33Val) linked
to familial amyloidotic polyneuropathy.";
Amyloid 11:121-124(2004).
[126]
VARIANTS SER-26; CYS-53 AND ALA-114, VARIANTS AMYL-TTR GLU-67; HIS-78;
ALA-80 AND TYR-97, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15217993; DOI=10.1373/clinchem.2004.033266;
Bergen H.R. III, Zeldenrust S.R., Butz M.L., Snow D.S., Dyck P.J.,
Dyck P.J.B., Klein C.J., O'Brien J.F., Thibodeau S.N., Muddiman D.C.;
"Identification of transthyretin variants by sequential proteomic and
genomic analysis.";
Clin. Chem. 50:1544-1552(2004).
[127]
VARIANT AMYL-TTR GLY-81.
PubMed=17453626; DOI=10.1080/13506120601116625;
Rosenzweig M., Skinner M., Prokaeva T., Theberge R., Costello C.,
Drachman B.M., Connors L.H.;
"A new transthyretin variant (Glu61Gly) associated with
cardiomyopathy.";
Amyloid 14:65-71(2007).
[128]
VARIANT AMYL-TTR SER-144.
PubMed=17577687; DOI=10.1080/13506120701259895;
Bergstroem J., Patrosso M.C., Colussi G., Salvadore M., Penco S.,
Lando G., Marocchi A., Ueda A., Nakamura M., Ando Y.;
"A novel type of familial transthyretin amyloidosis, ATTR Asn124Ser,
with co-localization of kappa light chains.";
Amyloid 14:141-145(2007).
[129]
VARIANTS AMYL-TTR PRO-32; ILE-40; SER-44; ALA-50; MET-50; LEU-53;
VAL-53; PRO-56; THR-65; ALA-67; ALA-69; ILE-69; ALA-80; LEU-84;
LEU-88; ALA-91; TYR-97; PHE-98; SER-104; ASN-104; THR-104; ALA-114;
GLY-117; ASN-126; MET-127; VAL-127; MET-131 AND ILE-142, VARIANTS
ILE-33; SER-121 AND THR-129, AND VARIANT CHICAGO MET-139.
PubMed=17503405; DOI=10.1002/elps.200600840;
Altland K., Benson M.D., Costello C.E., Ferlini A., Hazenberg B.P.C.,
Hund E., Kristen A.V., Linke R.P., Merlini G., Salvi F., Saraiva M.J.,
Singer R., Skinner M., Winter P.;
"Genetic microheterogeneity of human transthyretin detected by IEF.";
Electrophoresis 28:2053-2064(2007).
[130]
VARIANT AMYL-TTR VAL-58.
PubMed=17635579; DOI=10.1111/j.1365-2362.2007.01836.x;
Augustin S., Llige D., Andreu A., Gonzalez A., Genesca J.;
"Familial amyloidosis in a large Spanish kindred resulting from a D38V
mutation in the transthyretin gene.";
Eur. J. Clin. Invest. 37:673-678(2007).
[131]
VARIANT AMYL-TTR ARG-70.
PubMed=23317988; DOI=10.1016/j.jaad.2012.07.026;
Dekmezian M.S., Tschen J.A., Cho-Vega J.H.;
"Delayed diagnosis of transthyretin amyloidosis with a novel mutation
(c.210T>A) in the transthyretin gene.";
J. Am. Acad. Dermatol. 68:E49-E51(2013).
-!- FUNCTION: Thyroid hormone-binding protein. Probably transports
thyroxine from the bloodstream to the brain.
{ECO:0000269|PubMed:3714052}.
-!- SUBUNIT: Homotetramer. Dimer of dimers. In the homotetramer,
subunits assemble around a central channel that can accommodate
two ligand molecules. Interacts with RBP4.
{ECO:0000269|PubMed:10052934, ECO:0000269|PubMed:11243784,
ECO:0000269|PubMed:11560492, ECO:0000269|PubMed:12820260,
ECO:0000269|PubMed:14583036, ECO:0000269|PubMed:14711308,
ECO:0000269|PubMed:15735344, ECO:0000269|PubMed:15769474,
ECO:0000269|PubMed:15826192, ECO:0000269|PubMed:18095641,
ECO:0000269|PubMed:18155178, ECO:0000269|PubMed:18811132,
ECO:0000269|PubMed:19021760}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-711909, EBI-711909;
Q15109:AGER; NbExp=2; IntAct=EBI-711909, EBI-1646426;
Q01850:CDR2; NbExp=3; IntAct=EBI-711909, EBI-1181367;
P25713:MT3; NbExp=3; IntAct=EBI-711909, EBI-8084264;
Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-711909, EBI-10172876;
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasm.
-!- TISSUE SPECIFICITY: Detected in serum and cerebrospinal fluid (at
protein level). Highly expressed in choroid plexus epithelial
cells. Detected in retina pigment epithelium and liver.
{ECO:0000269|PubMed:10328977, ECO:0000269|PubMed:3714052}.
-!- DOMAIN: Each monomer has two 4-stranded beta sheets and the shape
of a prolate ellipsoid. Antiparallel beta-sheet interactions link
monomers into dimers. A short loop from each monomer forms the
main dimer-dimer interaction. These two pairs of loops separate
the opposed, convex beta-sheets of the dimers to form an internal
channel.
-!- PTM: Not glycosylated under normal conditions. Following
unfolding, caused for example by variant AMYL-TTR 'Gly-38', the
cryptic Asn-118 site is exposed and glycosylated by STT3B-
containing OST complex, leading to its degradation by the ER-
associated degradation (ERAD) pathway.
{ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19167329}.
-!- DISEASE: Amyloidosis, transthyretin-related (AMYL-TTR)
[MIM:105210]: A hereditary generalized amyloidosis due to
transthyretin amyloid deposition. Protein fibrils can form in
different tissues leading to amyloid polyneuropathies, amyloidotic
cardiomyopathy, carpal tunnel syndrome, systemic senile
amyloidosis. The disease includes leptomeningeal amyloidosis that
is characterized by primary involvement of the central nervous
system. Neuropathologic examination shows amyloid in the walls of
leptomeningeal vessels, in pia arachnoid, and subpial deposits.
Some patients also develop vitreous amyloid deposition that leads
to visual impairment (oculoleptomeningeal amyloidosis). Clinical
features include seizures, stroke-like episodes, dementia,
psychomotor deterioration, variable amyloid deposition in the
vitreous humor. {ECO:0000269|PubMed:10036587,
ECO:0000269|PubMed:10071047, ECO:0000269|PubMed:10211412,
ECO:0000269|PubMed:10436378, ECO:0000269|PubMed:10439117,
ECO:0000269|PubMed:10611950, ECO:0000269|PubMed:10627135,
ECO:0000269|PubMed:10694917, ECO:0000269|PubMed:10842705,
ECO:0000269|PubMed:10842718, ECO:0000269|PubMed:10882995,
ECO:0000269|PubMed:11243784, ECO:0000269|PubMed:11445644,
ECO:0000269|PubMed:11866053, ECO:0000269|PubMed:12050338,
ECO:0000269|PubMed:12403615, ECO:0000269|PubMed:12557757,
ECO:0000269|PubMed:12771253, ECO:0000269|PubMed:1301926,
ECO:0000269|PubMed:1351039, ECO:0000269|PubMed:1362222,
ECO:0000269|PubMed:1436517, ECO:0000269|PubMed:1517749,
ECO:0000269|PubMed:1520326, ECO:0000269|PubMed:1520336,
ECO:0000269|PubMed:15214015, ECO:0000269|PubMed:15217993,
ECO:0000269|PubMed:1544214, ECO:0000269|PubMed:15478468,
ECO:0000269|PubMed:1570831, ECO:0000269|PubMed:15735344,
ECO:0000269|PubMed:16185074, ECO:0000269|PubMed:1656975,
ECO:0000269|PubMed:16627944, ECO:0000269|PubMed:1734866,
ECO:0000269|PubMed:17453626, ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:17577687, ECO:0000269|PubMed:17635579,
ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:1932142,
ECO:0000269|PubMed:2046936, ECO:0000269|PubMed:2161654,
ECO:0000269|PubMed:23317988, ECO:0000269|PubMed:2363717,
ECO:0000269|PubMed:2891727, ECO:0000269|PubMed:3022108,
ECO:0000269|PubMed:3135807, ECO:0000269|PubMed:3722385,
ECO:0000269|PubMed:3818577, ECO:0000269|PubMed:6487335,
ECO:0000269|PubMed:6583672, ECO:0000269|PubMed:6651852,
ECO:0000269|PubMed:7655883, ECO:0000269|PubMed:7850982,
ECO:0000269|PubMed:7910950, ECO:0000269|PubMed:7914929,
ECO:0000269|PubMed:7923855, ECO:0000269|PubMed:8019560,
ECO:0000269|PubMed:8038017, ECO:0000269|PubMed:8081397,
ECO:0000269|PubMed:8095302, ECO:0000269|PubMed:8133316,
ECO:0000269|PubMed:8257997, ECO:0000269|PubMed:8352764,
ECO:0000269|PubMed:8382610, ECO:0000269|PubMed:8428915,
ECO:0000269|PubMed:8579098, ECO:0000269|PubMed:8990019,
ECO:0000269|PubMed:9066351, ECO:0000269|PubMed:9605286,
ECO:0000269|PubMed:9733771, ECO:0000269|Ref.90}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Hyperthyroxinemia, dystransthyretinemic (DTTRH)
[MIM:145680]: A condition characterized by elevation of total and
free thyroxine in healthy, euthyroid persons without detectable
binding protein abnormalities. {ECO:0000269|PubMed:1979335}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Carpal tunnel syndrome 1 (CTS1) [MIM:115430]: A condition
characterized by entrapment of the median nerve within the carpal
tunnel. Symptoms include burning pain and paresthesias involving
the ventral surface of the hand and fingers which may radiate
proximally. Impairment of sensation in the distribution of the
median nerve and thenar muscle atrophy may occur. This condition
may be associated with repetitive occupational trauma, wrist
injuries, amyloid neuropathies, rheumatoid arthritis.
{ECO:0000269|PubMed:8309582}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Tetramer dissociation and partial unfolding leads
to the formation of aggregates and amyloid fibrils. Small
molecules that occupy at least one of the thyroid hormone binding
sites stabilize the tetramer, and thereby stabilize the native
state and protect against misfolding and the formation of amyloid
fibrils.
-!- MISCELLANEOUS: Two binding sites for thyroxine are located in the
channel. Less than 1% of plasma prealbumin molecules are normally
involved in thyroxine transport. L-thyroxine binds to the
transthyretin by an order of magnitude stronger than does the
triiodo-L-thyronine. Thyroxine-binding globulin is the major
carrier protein for thyroid hormones in man.
-!- MISCELLANEOUS: About 40% of plasma transthyretin circulates in a
tight protein-protein complex with the plasma retinol-binding
protein (RBP). The formation of the complex with RBP stabilizes
the binding of retinol to RBP and decreases the glomerular
filtration and renal catabolism of the relatively small RBP
molecule. There is evidence for 2 binding sites for RBP, one
possibly being a region that includes Ile-104, located on the
outer surface of the transthyretin molecule.
-!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Transthyretin entry;
URL="https://en.wikipedia.org/wiki/Transthyretin";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; K02091; AAA60011.1; -; mRNA.
EMBL; M10605; AAA60012.1; -; mRNA.
EMBL; M11518; AAA98771.1; -; Genomic_DNA.
EMBL; M11844; AAA60013.1; -; Genomic_DNA.
EMBL; X59498; CAA42087.1; -; mRNA.
EMBL; D00096; BAA00059.1; -; mRNA.
EMBL; M15517; AAA60018.1; -; Genomic_DNA.
EMBL; M15515; AAA60018.1; JOINED; Genomic_DNA.
EMBL; M15516; AAA60018.1; JOINED; Genomic_DNA.
EMBL; U19780; AAA73473.1; -; mRNA.
EMBL; AF162690; AAD45014.1; -; mRNA.
EMBL; AK312051; BAG34987.1; -; mRNA.
EMBL; BT007189; AAP35853.1; -; mRNA.
EMBL; CR456908; CAG33189.1; -; mRNA.
EMBL; CH471088; EAX01264.1; -; Genomic_DNA.
EMBL; BC005310; AAH05310.1; -; mRNA.
EMBL; BC020791; AAH20791.1; -; mRNA.
EMBL; S63185; AAD14937.2; -; Genomic_DNA.
EMBL; S72385; AAD14098.1; -; Genomic_DNA.
EMBL; M11714; AAA61181.1; -; mRNA.
EMBL; M63285; AAA36784.1; -; Genomic_DNA.
CCDS; CCDS11899.1; -.
PIR; A91532; VBHU.
RefSeq; NP_000362.1; NM_000371.3.
UniGene; Hs.427202; -.
PDB; 1BM7; X-ray; 2.00 A; A/B=21-147.
PDB; 1BMZ; X-ray; 2.00 A; A/B=21-143.
PDB; 1BZ8; X-ray; 2.00 A; A/B=21-147.
PDB; 1BZD; X-ray; 1.90 A; A/B=21-147.
PDB; 1BZE; X-ray; 1.80 A; A/B=21-147.
PDB; 1DVQ; X-ray; 2.00 A; A/B=21-144.
PDB; 1DVS; X-ray; 2.00 A; A/B=21-144.
PDB; 1DVT; X-ray; 1.90 A; A/B=21-144.
PDB; 1DVU; X-ray; 1.90 A; A/B=21-144.
PDB; 1DVX; X-ray; 2.00 A; A/B=21-144.
PDB; 1DVY; X-ray; 1.90 A; A/B=21-144.
PDB; 1DVZ; X-ray; 1.90 A; A/B=21-144.
PDB; 1E3F; X-ray; 1.90 A; A/B=21-145.
PDB; 1E4H; X-ray; 1.80 A; A/B=21-147.
PDB; 1E5A; X-ray; 1.80 A; A/B=21-147.
PDB; 1ETA; X-ray; 1.70 A; 1/2=21-147.
PDB; 1ETB; X-ray; 1.70 A; 1/2=21-147.
PDB; 1F41; X-ray; 1.30 A; A/B=21-147.
PDB; 1F64; Model; -; A=21-147.
PDB; 1F86; X-ray; 1.10 A; A/B=30-144.
PDB; 1FH2; X-ray; 1.80 A; A/B=21-147.
PDB; 1FHN; X-ray; 1.75 A; A/B=21-147.
PDB; 1G1O; X-ray; 2.30 A; A/B/C/D=21-147.
PDB; 1GKO; X-ray; 2.10 A; A/B/C/D=21-147.
PDB; 1ICT; X-ray; 3.00 A; A/B/C/D/E/F/G/H=21-147.
PDB; 1III; X-ray; 2.00 A; A/B=21-147.
PDB; 1IIK; X-ray; 2.00 A; A/B=21-147.
PDB; 1IJN; X-ray; 1.70 A; A/B=21-147.
PDB; 1QAB; X-ray; 3.20 A; A/B/C/D=21-147.
PDB; 1QWH; X-ray; 1.36 A; A/B=31-147.
PDB; 1RLB; X-ray; 3.10 A; A/B/C/D=21-147.
PDB; 1SOK; X-ray; 1.60 A; A/B=21-147.
PDB; 1SOQ; X-ray; 2.10 A; A/B/C/D=21-147.
PDB; 1THA; X-ray; 2.00 A; A/B=21-147.
PDB; 1THC; X-ray; 2.30 A; A/B=21-147.
PDB; 1TLM; X-ray; 1.90 A; A/B=21-147.
PDB; 1TSH; X-ray; 1.70 A; A/B=21-147.
PDB; 1TT6; X-ray; 1.80 A; A/B=21-147.
PDB; 1TTA; X-ray; 1.70 A; A/B=21-147.
PDB; 1TTB; X-ray; 1.70 A; A/B=21-147.
PDB; 1TTC; X-ray; 1.70 A; A/B=21-147.
PDB; 1TTR; X-ray; 1.90 A; A/B=21-147.
PDB; 1TYR; X-ray; 1.80 A; A/B=21-147.
PDB; 1TZ8; X-ray; 1.85 A; A/B/C/D=21-147.
PDB; 1U21; X-ray; 1.69 A; A/B=21-147.
PDB; 1X7S; X-ray; 1.55 A; A/B=21-147.
PDB; 1X7T; X-ray; 1.60 A; A/B=21-147.
PDB; 1Y1D; X-ray; 1.70 A; A/B=21-147.
PDB; 1Z7J; X-ray; 2.20 A; A/B=21-147.
PDB; 1ZCR; X-ray; 1.80 A; A/B=21-147.
PDB; 1ZD6; X-ray; 1.90 A; A/B=21-147.
PDB; 2B14; X-ray; 2.00 A; A/B=21-147.
PDB; 2B15; X-ray; 1.70 A; A/B=21-147.
PDB; 2B16; X-ray; 1.75 A; A/B=21-147.
PDB; 2B77; X-ray; 1.70 A; A/B=21-147.
PDB; 2B9A; X-ray; 1.54 A; A/B=21-147.
PDB; 2F7I; X-ray; 1.60 A; A/B=21-147.
PDB; 2F8I; X-ray; 1.54 A; A/B=21-147.
PDB; 2FBR; X-ray; 1.46 A; A/B=21-147.
PDB; 2FLM; X-ray; 1.65 A; A/B=21-147.
PDB; 2G3X; X-ray; 1.58 A; A/B=21-147.
PDB; 2G3Z; X-ray; 1.90 A; A/B=21-147.
PDB; 2G4E; X-ray; 2.17 A; A/B=21-147.
PDB; 2G4G; X-ray; 1.85 A; A/B=21-147.
PDB; 2G5U; X-ray; 1.80 A; A/B=21-147.
PDB; 2G9K; X-ray; 1.85 A; A/B=21-147.
PDB; 2GAB; X-ray; 1.85 A; A/B=21-147.
PDB; 2H4E; X-ray; 1.45 A; A/B=21-147.
PDB; 2M5N; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=125-135.
PDB; 2NBO; NMR; -; A=21-147.
PDB; 2NBP; NMR; -; A=21-147.
PDB; 2NOY; X-ray; 1.80 A; A/B=21-147.
PDB; 2PAB; X-ray; 1.80 A; A/B=21-147.
PDB; 2QEL; X-ray; 2.29 A; A/B/C/D=21-147.
PDB; 2QGB; X-ray; 1.40 A; A/B=21-147.
PDB; 2QGC; X-ray; 1.30 A; A/B=21-147.
PDB; 2QGD; X-ray; 1.50 A; A/B=21-147.
PDB; 2QGE; X-ray; 1.45 A; A/B=21-147.
PDB; 2ROX; X-ray; 2.00 A; A/B=21-147.
PDB; 2ROY; X-ray; 2.20 A; A/B=21-147.
PDB; 2TRH; X-ray; 1.90 A; A/B=21-147.
PDB; 2TRY; X-ray; 2.00 A; A/B=21-147.
PDB; 2WQA; X-ray; 2.85 A; A/B/C/D=21-147.
PDB; 3A4D; X-ray; 2.00 A; A/B=21-147.
PDB; 3A4E; X-ray; 1.70 A; A/B=21-147.
PDB; 3A4F; X-ray; 1.99 A; A/B=21-147.
PDB; 3B56; X-ray; 1.55 A; A/B=21-147.
PDB; 3BSZ; X-ray; 3.38 A; A/B/C/D=21-147.
PDB; 3BT0; X-ray; 1.59 A; A/B=21-147.
PDB; 3CBR; X-ray; 1.70 A; A/B=21-147.
PDB; 3CFM; X-ray; 1.60 A; A/B=30-147.
PDB; 3CFN; X-ray; 1.87 A; A/B=30-147.
PDB; 3CFQ; X-ray; 2.09 A; A/B=30-147.
PDB; 3CFT; X-ray; 1.87 A; A/B=30-147.
PDB; 3CN0; X-ray; 1.52 A; A/B=21-147.
PDB; 3CN1; X-ray; 1.52 A; A/B=21-147.
PDB; 3CN2; X-ray; 1.52 A; A/B=21-147.
PDB; 3CN3; X-ray; 1.80 A; A/B=21-147.
PDB; 3CN4; X-ray; 1.40 A; A/B=21-147.
PDB; 3CXF; X-ray; 2.30 A; A/B=21-147.
PDB; 3D2T; X-ray; 1.85 A; A/B=21-147.
PDB; 3D7P; X-ray; 1.72 A; A/B=21-147.
PDB; 3DGD; X-ray; 1.38 A; A/B/C/D=21-147.
PDB; 3DID; X-ray; 1.78 A; A/B/C/D=21-147.
PDB; 3DJR; X-ray; 2.02 A; A/B=21-147.
PDB; 3DJS; X-ray; 1.80 A; A/B=21-147.
PDB; 3DJT; X-ray; 2.30 A; A/B=21-147.
PDB; 3DJZ; X-ray; 1.82 A; A/B=21-147.
PDB; 3DK0; X-ray; 1.87 A; A/B=21-147.
PDB; 3DK2; X-ray; 2.35 A; A/B=21-147.
PDB; 3DO4; X-ray; 2.40 A; A/B/C/D/E/F/G/H=21-147.
PDB; 3ESN; X-ray; 1.35 A; A/B=21-147.
PDB; 3ESO; X-ray; 1.31 A; A/B=21-147.
PDB; 3ESP; X-ray; 1.31 A; A/B=21-147.
PDB; 3FC8; X-ray; 1.85 A; A/B=21-144.
PDB; 3FCB; X-ray; 1.80 A; A/B=21-144.
PDB; 3GLZ; X-ray; 1.78 A; A/B=21-147.
PDB; 3GPS; X-ray; 1.78 A; A/B/C/D=21-147.
PDB; 3GRB; X-ray; 1.75 A; A/B/C/D=21-147.
PDB; 3GRG; X-ray; 1.90 A; A/B/C/D=21-147.
PDB; 3GS0; X-ray; 1.85 A; A/B=21-147.
PDB; 3GS4; X-ray; 1.78 A; A/B=21-147.
PDB; 3GS7; X-ray; 1.80 A; A/B=21-147.
PDB; 3HJ0; X-ray; 1.34 A; A/B=21-147.
PDB; 3I9A; X-ray; 1.65 A; A/B=21-147.
PDB; 3I9I; X-ray; 1.80 A; A/B=30-145.
PDB; 3I9P; X-ray; 1.90 A; A/B=30-145.
PDB; 3IMR; X-ray; 1.70 A; A/B=21-147.
PDB; 3IMS; X-ray; 1.40 A; A/B=21-147.
PDB; 3IMT; X-ray; 1.40 A; A/B=21-147.
PDB; 3IMU; X-ray; 1.40 A; A/B=21-147.
PDB; 3IMV; X-ray; 1.47 A; A/B=21-147.
PDB; 3IMW; X-ray; 1.31 A; A/B=21-147.
PDB; 3IPB; X-ray; 1.90 A; A/B=21-147.
PDB; 3IPE; X-ray; 1.40 A; A/B=21-147.
PDB; 3KGS; X-ray; 1.80 A; A/B=21-147.
PDB; 3KGT; X-ray; 1.95 A; A/B=21-147.
PDB; 3KGU; X-ray; 1.85 A; A/B=21-147.
PDB; 3M1O; X-ray; 1.20 A; A/B=21-147.
PDB; 3NEE; X-ray; 1.55 A; A/B=30-145.
PDB; 3NEO; X-ray; 2.00 A; A/B=30-145.
PDB; 3NES; X-ray; 1.75 A; A/B=30-145.
PDB; 3NEX; X-ray; 1.70 A; A/B=30-145.
PDB; 3NG5; X-ray; 1.70 A; A/B=21-147.
PDB; 3OZK; X-ray; 1.90 A; A/B=21-147.
PDB; 3OZL; X-ray; 1.90 A; A/B=21-147.
PDB; 3P3R; X-ray; 1.25 A; A/B=21-147.
PDB; 3P3S; X-ray; 1.60 A; A/B=21-147.
PDB; 3P3T; X-ray; 1.45 A; A/B=21-147.
PDB; 3P3U; X-ray; 1.50 A; A/B=21-147.
PDB; 3SSG; X-ray; 2.00 A; A=21-147.
PDB; 3TCT; X-ray; 1.30 A; A/B=21-147.
PDB; 3TFB; X-ray; 2.03 A; A/B=30-145.
PDB; 3U2I; X-ray; 1.70 A; A/B=32-147.
PDB; 3U2J; Neutron; 2.00 A; A/B=32-147.
PDB; 3W3B; X-ray; 1.90 A; A/B=21-147.
PDB; 4ABQ; X-ray; 1.70 A; A/B=21-144.
PDB; 4ABU; X-ray; 1.86 A; A/B=21-144.
PDB; 4ABV; X-ray; 1.80 A; A/B=21-144.
PDB; 4ABW; X-ray; 1.70 A; A/B=21-144.
PDB; 4AC2; X-ray; 1.81 A; A/B=21-144.
PDB; 4AC4; X-ray; 1.80 A; A/B=21-147.
PDB; 4ACT; X-ray; 1.80 A; A/B=21-147.
PDB; 4ANK; X-ray; 1.70 A; A/B=1-147.
PDB; 4D7B; X-ray; 1.15 A; A/B=21-147.
PDB; 4DER; X-ray; 1.90 A; A/B=30-145.
PDB; 4DES; X-ray; 1.75 A; A/B=30-145.
PDB; 4DET; X-ray; 2.05 A; A/B=30-145.
PDB; 4DEU; X-ray; 1.60 A; A/B=30-145.
PDB; 4DEW; X-ray; 1.90 A; A/B=1-147.
PDB; 4FI6; X-ray; 1.46 A; A/B=21-147.
PDB; 4FI7; X-ray; 1.40 A; A/B=21-147.
PDB; 4FI8; X-ray; 1.22 A; A/B=21-147.
PDB; 4HIQ; X-ray; 1.18 A; A/B=21-147.
PDB; 4HIS; X-ray; 1.20 A; A/B=21-147.
PDB; 4HJS; X-ray; 1.22 A; A/B=30-145.
PDB; 4HJT; X-ray; 1.45 A; A/B=21-147.
PDB; 4HJU; X-ray; 1.35 A; A/B=21-147.
PDB; 4I85; X-ray; 1.67 A; A/B=21-147.
PDB; 4I87; X-ray; 1.69 A; A/B=21-147.
PDB; 4I89; X-ray; 1.69 A; A/B=21-147.
PDB; 4IIZ; X-ray; 2.10 A; A/B=21-147.
PDB; 4IK6; X-ray; 2.00 A; A/B=21-147.
PDB; 4IK7; X-ray; 2.10 A; A/B=21-147.
PDB; 4IKI; X-ray; 2.00 A; A/B=21-147.
PDB; 4IKJ; X-ray; 2.10 A; A/B=21-147.
PDB; 4IKK; X-ray; 1.90 A; A/B=21-147.
PDB; 4IKL; X-ray; 1.90 A; A/B=21-147.
PDB; 4KY2; X-ray; 1.13 A; A/B=21-147.
PDB; 4L1S; X-ray; 1.50 A; A/B=21-147.
PDB; 4L1T; X-ray; 1.16 A; A/B=21-147.
PDB; 4MAS; X-ray; 1.22 A; A/B=21-147.
PDB; 4MRB; X-ray; 1.27 A; A/B=21-147.
PDB; 4MRC; X-ray; 1.54 A; A/B=22-147.
PDB; 4N85; X-ray; 1.60 A; A/B=1-147.
PDB; 4N86; X-ray; 2.00 A; A/B=1-147.
PDB; 4N87; X-ray; 1.79 A; A/B=1-147.
PDB; 4PM1; X-ray; 1.23 A; A/B=21-147.
PDB; 4PME; X-ray; 1.26 A; A/B=29-146.
PDB; 4PMF; X-ray; 1.35 A; A/B=29-145.
PDB; 4PVL; X-ray; 1.85 A; A/B=21-147.
PDB; 4PVM; Other; 2.00 A; A/B=21-147.
PDB; 4PVN; Other; 2.30 A; A/B=21-147.
PDB; 4PWE; X-ray; 1.40 A; A/B=1-147.
PDB; 4PWF; X-ray; 1.60 A; A/B=1-147.
PDB; 4PWG; X-ray; 1.80 A; A/B=1-147.
PDB; 4PWH; X-ray; 1.80 A; A/B=1-147.
PDB; 4PWI; X-ray; 1.49 A; A/B=1-147.
PDB; 4PWJ; X-ray; 1.55 A; A/B=1-147.
PDB; 4PWK; X-ray; 1.59 A; A/B=1-147.
PDB; 4QRF; X-ray; 1.80 A; A/B=1-147.
PDB; 4QXV; X-ray; 1.12 A; A/B=21-147.
PDB; 4QYA; X-ray; 1.70 A; A/B=21-147.
PDB; 4TKW; X-ray; 1.80 A; A/B=29-147.
PDB; 4TL4; X-ray; 1.75 A; A/B=29-147.
PDB; 4TL5; X-ray; 1.44 A; A/B=29-147.
PDB; 4TLK; X-ray; 1.44 A; A/B=29-147.
PDB; 4TLS; X-ray; 1.35 A; A/B=29-147.
PDB; 4TLT; X-ray; 1.70 A; A/B=29-147.
PDB; 4TLU; X-ray; 1.75 A; A/B=29-147.
PDB; 4TM9; X-ray; 1.70 A; A/B=29-147.
PDB; 4TNE; X-ray; 1.55 A; A/B=29-147.
PDB; 4TNF; X-ray; 1.60 A; A/B=29-147.
PDB; 4TNG; X-ray; 1.60 A; A/B=29-147.
PDB; 4TQ8; X-ray; 1.52 A; A/B=21-147.
PDB; 4TQH; X-ray; 1.51 A; A/B=21-147.
PDB; 4TQI; X-ray; 1.25 A; A/B=21-147.
PDB; 4TQP; X-ray; 1.58 A; A/B=21-147.
PDB; 4WNJ; X-ray; 1.40 A; A/B=21-147.
PDB; 4WNS; X-ray; 1.40 A; A/B=21-147.
PDB; 4WO0; X-ray; 1.34 A; A/B=21-147.
PDB; 4Y9B; X-ray; 1.40 A; A/B=1-147.
PDB; 4Y9C; X-ray; 1.49 A; A/B=1-147.
PDB; 4Y9E; X-ray; 1.49 A; A/B=1-147.
PDB; 4Y9F; X-ray; 1.50 A; A/B=1-147.
PDB; 4Y9G; X-ray; 1.89 A; A/B=1-147.
PDB; 4YDM; X-ray; 1.25 A; A/B=21-147.
PDB; 4YDN; X-ray; 1.35 A; A/B=21-147.
PDB; 5A6I; X-ray; 1.86 A; A=21-147.
PDB; 5AKS; X-ray; 1.25 A; A/B=21-147.
PDB; 5AKT; X-ray; 1.35 A; A/B=21-147.
PDB; 5AKV; X-ray; 1.52 A; A/B=21-147.
PDB; 5AL0; X-ray; 1.39 A; A/B=21-147.
PDB; 5AL8; X-ray; 1.50 A; A/B=21-147.
PDB; 5AYT; X-ray; 1.40 A; A/B=1-147.
PDB; 5BOJ; X-ray; 1.75 A; A/B=21-147.
PDB; 5CLX; X-ray; 1.28 A; A/B=21-147.
PDB; 5CLY; X-ray; 1.23 A; A/B=21-147.
PDB; 5CLZ; X-ray; 1.22 A; A/B=21-147.
PDB; 5CM1; X-ray; 1.22 A; A/B=21-147.
PDB; 5CN3; X-ray; 1.30 A; A/B=21-147.
PDB; 5CNH; X-ray; 1.42 A; A/B=21-147.
PDB; 5CR1; X-ray; 1.54 A; A/B=30-145.
PDB; 5DEJ; X-ray; 1.37 A; A/B=30-145.
PDB; 5DWP; X-ray; 1.20 A; A/B=30-145.
PDB; 5E23; X-ray; 1.41 A; A/B=21-147.
PDB; 5E4A; X-ray; 1.33 A; A/B=10-146.
PDB; 5E4O; X-ray; 1.50 A; A/B=30-146.
PDB; 5EN3; X-ray; 1.25 A; A/B=21-147.
PDB; 5EZP; X-ray; 2.50 A; A/B/C/D/E/F/G/H=26-147.
PDB; 5FO2; X-ray; 1.45 A; A/B=21-147.
PDB; 5FW6; X-ray; 1.30 A; A/B=21-147.
PDB; 5FW7; X-ray; 1.20 A; A/B=21-147.
PDB; 5FW8; X-ray; 1.60 A; A/B=21-147.
PDB; 5H0V; X-ray; 1.58 A; A/B/C/D=31-147.
PDB; 5H0W; X-ray; 1.90 A; A=31-147.
PDB; 5H0X; X-ray; 1.57 A; A/B=31-147.
PDB; 5H0Y; X-ray; 1.80 A; A=31-147.
PDB; 5H0Z; X-ray; 1.74 A; A=31-147.
PDB; 5HJG; X-ray; 1.40 A; A/B=21-147.
PDB; 5IHH; X-ray; 1.35 A; A/B=21-147.
PDB; 5JID; X-ray; 1.20 A; A/B=21-147.
PDB; 5JIM; X-ray; 1.26 A; A/B=21-147.
PDB; 5JIQ; X-ray; 1.45 A; A/B=21-147.
PDB; 5K1J; X-ray; 1.69 A; A/B=30-145.
PDB; 5K1N; X-ray; 1.81 A; A/B=30-147.
PDB; 5L4F; X-ray; 1.48 A; A/B=21-147.
PDB; 5L4I; X-ray; 1.45 A; A/B=21-147.
PDB; 5L4J; X-ray; 1.62 A; A/B=21-147.
PDB; 5L4M; X-ray; 1.58 A; A/B=21-147.
PDB; 5LLL; X-ray; 1.42 A; A/B=21-147.
PDB; 5LLV; X-ray; 1.70 A; A/B/C/D=21-147.
PDB; 5TTR; X-ray; 2.70 A; A/B/C/D/E/F/G/H=21-147.
PDBsum; 1BM7; -.
PDBsum; 1BMZ; -.
PDBsum; 1BZ8; -.
PDBsum; 1BZD; -.
PDBsum; 1BZE; -.
PDBsum; 1DVQ; -.
PDBsum; 1DVS; -.
PDBsum; 1DVT; -.
PDBsum; 1DVU; -.
PDBsum; 1DVX; -.
PDBsum; 1DVY; -.
PDBsum; 1DVZ; -.
PDBsum; 1E3F; -.
PDBsum; 1E4H; -.
PDBsum; 1E5A; -.
PDBsum; 1ETA; -.
PDBsum; 1ETB; -.
PDBsum; 1F41; -.
PDBsum; 1F64; -.
PDBsum; 1F86; -.
PDBsum; 1FH2; -.
PDBsum; 1FHN; -.
PDBsum; 1G1O; -.
PDBsum; 1GKO; -.
PDBsum; 1ICT; -.
PDBsum; 1III; -.
PDBsum; 1IIK; -.
PDBsum; 1IJN; -.
PDBsum; 1QAB; -.
PDBsum; 1QWH; -.
PDBsum; 1RLB; -.
PDBsum; 1SOK; -.
PDBsum; 1SOQ; -.
PDBsum; 1THA; -.
PDBsum; 1THC; -.
PDBsum; 1TLM; -.
PDBsum; 1TSH; -.
PDBsum; 1TT6; -.
PDBsum; 1TTA; -.
PDBsum; 1TTB; -.
PDBsum; 1TTC; -.
PDBsum; 1TTR; -.
PDBsum; 1TYR; -.
PDBsum; 1TZ8; -.
PDBsum; 1U21; -.
PDBsum; 1X7S; -.
PDBsum; 1X7T; -.
PDBsum; 1Y1D; -.
PDBsum; 1Z7J; -.
PDBsum; 1ZCR; -.
PDBsum; 1ZD6; -.
PDBsum; 2B14; -.
PDBsum; 2B15; -.
PDBsum; 2B16; -.
PDBsum; 2B77; -.
PDBsum; 2B9A; -.
PDBsum; 2F7I; -.
PDBsum; 2F8I; -.
PDBsum; 2FBR; -.
PDBsum; 2FLM; -.
PDBsum; 2G3X; -.
PDBsum; 2G3Z; -.
PDBsum; 2G4E; -.
PDBsum; 2G4G; -.
PDBsum; 2G5U; -.
PDBsum; 2G9K; -.
PDBsum; 2GAB; -.
PDBsum; 2H4E; -.
PDBsum; 2M5N; -.
PDBsum; 2NBO; -.
PDBsum; 2NBP; -.
PDBsum; 2NOY; -.
PDBsum; 2PAB; -.
PDBsum; 2QEL; -.
PDBsum; 2QGB; -.
PDBsum; 2QGC; -.
PDBsum; 2QGD; -.
PDBsum; 2QGE; -.
PDBsum; 2ROX; -.
PDBsum; 2ROY; -.
PDBsum; 2TRH; -.
PDBsum; 2TRY; -.
PDBsum; 2WQA; -.
PDBsum; 3A4D; -.
PDBsum; 3A4E; -.
PDBsum; 3A4F; -.
PDBsum; 3B56; -.
PDBsum; 3BSZ; -.
PDBsum; 3BT0; -.
PDBsum; 3CBR; -.
PDBsum; 3CFM; -.
PDBsum; 3CFN; -.
PDBsum; 3CFQ; -.
PDBsum; 3CFT; -.
PDBsum; 3CN0; -.
PDBsum; 3CN1; -.
PDBsum; 3CN2; -.
PDBsum; 3CN3; -.
PDBsum; 3CN4; -.
PDBsum; 3CXF; -.
PDBsum; 3D2T; -.
PDBsum; 3D7P; -.
PDBsum; 3DGD; -.
PDBsum; 3DID; -.
PDBsum; 3DJR; -.
PDBsum; 3DJS; -.
PDBsum; 3DJT; -.
PDBsum; 3DJZ; -.
PDBsum; 3DK0; -.
PDBsum; 3DK2; -.
PDBsum; 3DO4; -.
PDBsum; 3ESN; -.
PDBsum; 3ESO; -.
PDBsum; 3ESP; -.
PDBsum; 3FC8; -.
PDBsum; 3FCB; -.
PDBsum; 3GLZ; -.
PDBsum; 3GPS; -.
PDBsum; 3GRB; -.
PDBsum; 3GRG; -.
PDBsum; 3GS0; -.
PDBsum; 3GS4; -.
PDBsum; 3GS7; -.
PDBsum; 3HJ0; -.
PDBsum; 3I9A; -.
PDBsum; 3I9I; -.
PDBsum; 3I9P; -.
PDBsum; 3IMR; -.
PDBsum; 3IMS; -.
PDBsum; 3IMT; -.
PDBsum; 3IMU; -.
PDBsum; 3IMV; -.
PDBsum; 3IMW; -.
PDBsum; 3IPB; -.
PDBsum; 3IPE; -.
PDBsum; 3KGS; -.
PDBsum; 3KGT; -.
PDBsum; 3KGU; -.
PDBsum; 3M1O; -.
PDBsum; 3NEE; -.
PDBsum; 3NEO; -.
PDBsum; 3NES; -.
PDBsum; 3NEX; -.
PDBsum; 3NG5; -.
PDBsum; 3OZK; -.
PDBsum; 3OZL; -.
PDBsum; 3P3R; -.
PDBsum; 3P3S; -.
PDBsum; 3P3T; -.
PDBsum; 3P3U; -.
PDBsum; 3SSG; -.
PDBsum; 3TCT; -.
PDBsum; 3TFB; -.
PDBsum; 3U2I; -.
PDBsum; 3U2J; -.
PDBsum; 3W3B; -.
PDBsum; 4ABQ; -.
PDBsum; 4ABU; -.
PDBsum; 4ABV; -.
PDBsum; 4ABW; -.
PDBsum; 4AC2; -.
PDBsum; 4AC4; -.
PDBsum; 4ACT; -.
PDBsum; 4ANK; -.
PDBsum; 4D7B; -.
PDBsum; 4DER; -.
PDBsum; 4DES; -.
PDBsum; 4DET; -.
PDBsum; 4DEU; -.
PDBsum; 4DEW; -.
PDBsum; 4FI6; -.
PDBsum; 4FI7; -.
PDBsum; 4FI8; -.
PDBsum; 4HIQ; -.
PDBsum; 4HIS; -.
PDBsum; 4HJS; -.
PDBsum; 4HJT; -.
PDBsum; 4HJU; -.
PDBsum; 4I85; -.
PDBsum; 4I87; -.
PDBsum; 4I89; -.
PDBsum; 4IIZ; -.
PDBsum; 4IK6; -.
PDBsum; 4IK7; -.
PDBsum; 4IKI; -.
PDBsum; 4IKJ; -.
PDBsum; 4IKK; -.
PDBsum; 4IKL; -.
PDBsum; 4KY2; -.
PDBsum; 4L1S; -.
PDBsum; 4L1T; -.
PDBsum; 4MAS; -.
PDBsum; 4MRB; -.
PDBsum; 4MRC; -.
PDBsum; 4N85; -.
PDBsum; 4N86; -.
PDBsum; 4N87; -.
PDBsum; 4PM1; -.
PDBsum; 4PME; -.
PDBsum; 4PMF; -.
PDBsum; 4PVL; -.
PDBsum; 4PVM; -.
PDBsum; 4PVN; -.
PDBsum; 4PWE; -.
PDBsum; 4PWF; -.
PDBsum; 4PWG; -.
PDBsum; 4PWH; -.
PDBsum; 4PWI; -.
PDBsum; 4PWJ; -.
PDBsum; 4PWK; -.
PDBsum; 4QRF; -.
PDBsum; 4QXV; -.
PDBsum; 4QYA; -.
PDBsum; 4TKW; -.
PDBsum; 4TL4; -.
PDBsum; 4TL5; -.
PDBsum; 4TLK; -.
PDBsum; 4TLS; -.
PDBsum; 4TLT; -.
PDBsum; 4TLU; -.
PDBsum; 4TM9; -.
PDBsum; 4TNE; -.
PDBsum; 4TNF; -.
PDBsum; 4TNG; -.
PDBsum; 4TQ8; -.
PDBsum; 4TQH; -.
PDBsum; 4TQI; -.
PDBsum; 4TQP; -.
PDBsum; 4WNJ; -.
PDBsum; 4WNS; -.
PDBsum; 4WO0; -.
PDBsum; 4Y9B; -.
PDBsum; 4Y9C; -.
PDBsum; 4Y9E; -.
PDBsum; 4Y9F; -.
PDBsum; 4Y9G; -.
PDBsum; 4YDM; -.
PDBsum; 4YDN; -.
PDBsum; 5A6I; -.
PDBsum; 5AKS; -.
PDBsum; 5AKT; -.
PDBsum; 5AKV; -.
PDBsum; 5AL0; -.
PDBsum; 5AL8; -.
PDBsum; 5AYT; -.
PDBsum; 5BOJ; -.
PDBsum; 5CLX; -.
PDBsum; 5CLY; -.
PDBsum; 5CLZ; -.
PDBsum; 5CM1; -.
PDBsum; 5CN3; -.
PDBsum; 5CNH; -.
PDBsum; 5CR1; -.
PDBsum; 5DEJ; -.
PDBsum; 5DWP; -.
PDBsum; 5E23; -.
PDBsum; 5E4A; -.
PDBsum; 5E4O; -.
PDBsum; 5EN3; -.
PDBsum; 5EZP; -.
PDBsum; 5FO2; -.
PDBsum; 5FW6; -.
PDBsum; 5FW7; -.
PDBsum; 5FW8; -.
PDBsum; 5H0V; -.
PDBsum; 5H0W; -.
PDBsum; 5H0X; -.
PDBsum; 5H0Y; -.
PDBsum; 5H0Z; -.
PDBsum; 5HJG; -.
PDBsum; 5IHH; -.
PDBsum; 5JID; -.
PDBsum; 5JIM; -.
PDBsum; 5JIQ; -.
PDBsum; 5K1J; -.
PDBsum; 5K1N; -.
PDBsum; 5L4F; -.
PDBsum; 5L4I; -.
PDBsum; 5L4J; -.
PDBsum; 5L4M; -.
PDBsum; 5LLL; -.
PDBsum; 5LLV; -.
PDBsum; 5TTR; -.
ProteinModelPortal; P02766; -.
SMR; P02766; -.
BioGrid; 113127; 51.
CORUM; P02766; -.
DIP; DIP-1083N; -.
IntAct; P02766; 48.
MINT; MINT-1374623; -.
STRING; 9606.ENSP00000237014; -.
BindingDB; P02766; -.
ChEMBL; CHEMBL3194; -.
DrugBank; DB07201; (2S)-3-[(9H-fluoren-9-ylideneamino)oxy]-2-methylpropanoic acid.
DrugBank; DB04474; 1-Anilino-8-Naphthalene Sulfonate.
DrugBank; DB07282; 3-({[(1Z)-(2-methoxyphenyl)methylidene]amino}oxy)propanoic acid.
DrugBank; DB07240; 3-[(9H-fluoren-9-ylideneamino)oxy]propanoic acid.
DrugBank; DB06885; 3-[({(1E)-[2-(trifluoromethyl)phenyl]methylidene}amino)oxy]propanoic acid.
DrugBank; DB07176; 5-aminonaphthalene-1-sulfonic acid.
DrugBank; DB00586; Diclofenac.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB00861; Diflunisal.
DrugBank; DB01093; Dimethyl sulfoxide.
DrugBank; DB02266; Flufenamic Acid.
DrugBank; DB05352; Fx-1006A.
DrugBank; DB01645; Genistein.
DrugBank; DB00451; Levothyroxine.
DrugBank; DB00279; Liothyronine.
DrugBank; DB01583; Liotrix.
DrugBank; DB05235; NRP409.
DrugBank; DB02179; O-Trifluoromethylphenyl Anthranilic Acid.
DrugBank; DB03167; Pentabromophenol.
DrugBank; DB02709; Resveratrol.
GuidetoPHARMACOLOGY; 2851; -.
iPTMnet; P02766; -.
PhosphoSitePlus; P02766; -.
BioMuta; TTR; -.
DMDM; 136464; -.
DOSAC-COBS-2DPAGE; P02766; -.
REPRODUCTION-2DPAGE; P02766; -.
SWISS-2DPAGE; P02766; -.
UCD-2DPAGE; P02766; -.
MaxQB; P02766; -.
PaxDb; P02766; -.
PeptideAtlas; P02766; -.
PRIDE; P02766; -.
TopDownProteomics; P02766; -.
DNASU; 7276; -.
Ensembl; ENST00000237014; ENSP00000237014; ENSG00000118271.
GeneID; 7276; -.
KEGG; hsa:7276; -.
UCSC; uc002kwx.5; human.
CTD; 7276; -.
DisGeNET; 7276; -.
EuPathDB; HostDB:ENSG00000118271.9; -.
GeneCards; TTR; -.
GeneReviews; TTR; -.
HGNC; HGNC:12405; TTR.
HPA; CAB002517; -.
HPA; CAB062567; -.
HPA; CAB073406; -.
HPA; HPA002550; -.
MalaCards; TTR; -.
MIM; 105210; phenotype.
MIM; 115430; phenotype.
MIM; 145680; phenotype.
MIM; 176300; gene.
neXtProt; NX_P02766; -.
OpenTargets; ENSG00000118271; -.
Orphanet; 85447; Familial amyloid polyneuropathy.
Orphanet; 85451; Transthyretin-related familial amyloid cardiomyopathy.
PharmGKB; PA37069; -.
eggNOG; KOG3006; Eukaryota.
eggNOG; COG2351; LUCA.
GeneTree; ENSGT00390000005321; -.
HOGENOM; HOG000251776; -.
HOVERGEN; HBG000285; -.
InParanoid; P02766; -.
KO; K20731; -.
PhylomeDB; P02766; -.
TreeFam; TF300210; -.
Reactome; R-HSA-2453864; Retinoid cycle disease events.
Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
Reactome; R-HSA-977225; Amyloid fiber formation.
ChiTaRS; TTR; human.
EvolutionaryTrace; P02766; -.
GeneWiki; Transthyretin; -.
GenomeRNAi; 7276; -.
PMAP-CutDB; P02766; -.
PRO; PR:P02766; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000118271; -.
CleanEx; HS_TTR; -.
ExpressionAtlas; P02766; baseline and differential.
Genevisible; P02766; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0070324; F:thyroid hormone binding; IBA:GO_Central.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0042572; P:retinol metabolic process; IEA:Ensembl.
GO; GO:0070327; P:thyroid hormone transport; IEA:InterPro.
GO; GO:0006810; P:transport; NAS:ProtInc.
Gene3D; 2.60.40.180; -; 1.
InterPro; IPR023418; Thyroxine_BS.
InterPro; IPR030178; Transthyretin.
InterPro; IPR000895; Transthyretin/HIU_hydrolase.
InterPro; IPR023416; Transthyretin/HIU_hydrolase_SF.
InterPro; IPR023419; Transthyretin_CS.
PANTHER; PTHR10395; PTHR10395; 1.
PANTHER; PTHR10395:SF19; PTHR10395:SF19; 1.
Pfam; PF00576; Transthyretin; 1.
PRINTS; PR00189; TRNSTHYRETIN.
SMART; SM00095; TR_THY; 1.
SUPFAM; SSF49472; SSF49472; 1.
PROSITE; PS00768; TRANSTHYRETIN_1; 1.
PROSITE; PS00769; TRANSTHYRETIN_2; 1.
1: Evidence at protein level;
3D-structure; Amyloid; Amyloidosis; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation;
Gamma-carboxyglutamic acid; Glycoprotein; Hormone; Neuropathy;
Phosphoprotein; Polymorphism; Reference proteome; Secreted; Signal;
Thyroid hormone; Transport.
SIGNAL 1 20 {ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:1517749,
ECO:0000269|PubMed:3135807,
ECO:0000269|PubMed:4607556,
ECO:0000269|PubMed:6583672,
ECO:0000269|PubMed:6651852}.
CHAIN 21 147 Transthyretin.
/FTId=PRO_0000035755.
REGION 135 139 Thyroid hormone binding.
BINDING 35 35 Thyroid hormones.
BINDING 74 74 Thyroid hormones.
MOD_RES 62 62 4-carboxyglutamate; in a patient with
Moyamoya disease.
{ECO:0000269|PubMed:18221012}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:P02767}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19167329}.
VARIANT 26 26 G -> S (common polymorphism;
dbSNP:rs1800458).
{ECO:0000269|PubMed:10211412,
ECO:0000269|PubMed:11866053,
ECO:0000269|PubMed:15217993,
ECO:0000269|PubMed:6300852,
ECO:0000269|PubMed:8019560}.
/FTId=VAR_007546.
VARIANT 30 30 C -> R (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918083).
{ECO:0000269|PubMed:1362222}.
/FTId=VAR_007547.
VARIANT 32 32 L -> P (in AMYL-TTR; dbSNP:rs121918094).
{ECO:0000269|PubMed:10071047,
ECO:0000269|PubMed:17503405}.
/FTId=VAR_038959.
VARIANT 33 33 M -> I. {ECO:0000269|PubMed:17503405}.
/FTId=VAR_038960.
VARIANT 38 38 D -> E (in AMYL-TTR; amyloid
polyneuropathy).
/FTId=VAR_007548.
VARIANT 38 38 D -> G (in AMYL-TTR; leptomeningeal
amyloidosis; leads to unfolding and
exposure of N-118 to glycosylation by
STT3B and subsequent degradation by the
ERAD pathway; dbSNP:rs121918098).
{ECO:0000269|PubMed:19167329,
ECO:0000269|PubMed:8579098}.
/FTId=VAR_007549.
VARIANT 40 40 V -> I (in AMYL-TTR; late-onset amyloid
polyneuropathy with carpal tunnel
syndrome; dbSNP:rs121918093).
{ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:8990019}.
/FTId=VAR_007550.
VARIANT 43 43 S -> N (in AMYL-TTR).
{ECO:0000269|PubMed:10439117}.
/FTId=VAR_038961.
VARIANT 44 44 P -> S (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs11541790).
{ECO:0000269|PubMed:17503405}.
/FTId=VAR_007551.
VARIANT 48 48 V -> M (in AMYL-TTR; amyloid
polyneuropathy).
{ECO:0000269|PubMed:10882995}.
/FTId=VAR_010658.
VARIANT 50 50 V -> A (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs79977247).
{ECO:0000269|PubMed:1544214,
ECO:0000269|PubMed:17503405}.
/FTId=VAR_007552.
VARIANT 50 50 V -> G (in AMYL-TTR; dbSNP:rs79977247).
{ECO:0000269|PubMed:9066351}.
/FTId=VAR_038962.
VARIANT 50 50 V -> L (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs28933979).
{ECO:0000269|PubMed:10611950,
ECO:0000269|PubMed:1520326}.
/FTId=VAR_007553.
VARIANT 50 50 V -> M (in AMYL-TTR; amyloid
polyneuropathy; by far the most frequent
mutation; dbSNP:rs28933979).
{ECO:0000269|PubMed:12050338,
ECO:0000269|PubMed:1517749,
ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:3022108,
ECO:0000269|PubMed:3818577,
ECO:0000269|PubMed:6583672,
ECO:0000269|PubMed:6651852,
ECO:0000269|PubMed:7655883,
ECO:0000269|PubMed:8382610,
ECO:0000269|PubMed:8428915}.
/FTId=VAR_007554.
VARIANT 53 53 F -> C (in a patient with amyloidosis).
{ECO:0000269|PubMed:12876326,
ECO:0000269|PubMed:15217993}.
/FTId=VAR_038963.
VARIANT 53 53 F -> I (in AMYL-TTR; Jewish 'SKO' amyloid
polyneuropathy; dbSNP:rs121918068).
{ECO:0000269|PubMed:6487335,
ECO:0000269|PubMed:8019560}.
/FTId=VAR_007555.
VARIANT 53 53 F -> L (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918068).
{ECO:0000269|PubMed:12050338,
ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:1932142,
ECO:0000269|PubMed:2046936}.
/FTId=VAR_007556.
VARIANT 53 53 F -> V (in AMYL-TTR; amyloid
polyneuropathy).
{ECO:0000269|PubMed:10611950,
ECO:0000269|PubMed:12050338,
ECO:0000269|PubMed:15478468,
ECO:0000269|PubMed:17503405}.
/FTId=VAR_038964.
VARIANT 54 54 R -> T (in AMYL-TTR).
{ECO:0000269|PubMed:9605286}.
/FTId=VAR_038965.
VARIANT 55 55 K -> N (in AMYL-TTR; amyloid
polyneuropathy).
{ECO:0000269|PubMed:7655883}.
/FTId=VAR_038966.
VARIANT 56 56 A -> P (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918077).
{ECO:0000269|PubMed:17503405}.
/FTId=VAR_007557.
VARIANT 58 58 D -> A (in AMYL-TTR).
{ECO:0000269|PubMed:10611950,
ECO:0000269|PubMed:11866053}.
/FTId=VAR_038967.
VARIANT 58 58 D -> V (in AMYL-TTR).
{ECO:0000269|PubMed:12050338,
ECO:0000269|PubMed:17635579}.
/FTId=VAR_038968.
VARIANT 61 61 W -> L (in AMYL-TTR).
{ECO:0000269|PubMed:11866053}.
/FTId=VAR_038969.
VARIANT 62 62 E -> D (in AMYL-TTR; dbSNP:rs11541796).
{ECO:0000269|PubMed:10036587}.
/FTId=VAR_038970.
VARIANT 62 62 E -> G (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs11541796).
{ECO:0000269|PubMed:2363717,
ECO:0000269|PubMed:7923855}.
/FTId=VAR_007558.
VARIANT 64 64 F -> S (in AMYL-TTR; dbSNP:rs104894665).
{ECO:0000269|PubMed:11866053,
ECO:0000269|PubMed:9818883}.
/FTId=VAR_038971.
VARIANT 65 65 A -> D (in AMYL-TTR; amyloid
cardiomyopathy; dbSNP:rs730881169).
/FTId=VAR_007559.
VARIANT 65 65 A -> S (in AMYL-TTR).
{ECO:0000269|PubMed:10842718}.
/FTId=VAR_038972.
VARIANT 65 65 A -> T (in AMYL-TTR; amyloid
cardiomyopathy; dbSNP:rs121918078).
{ECO:0000269|PubMed:1570831,
ECO:0000269|PubMed:17503405}.
/FTId=VAR_007560.
VARIANT 67 67 G -> A (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918090).
{ECO:0000269|PubMed:17503405,
ECO:0000269|Ref.90}.
/FTId=VAR_007561.
VARIANT 67 67 G -> E (in AMYL-TTR).
{ECO:0000269|PubMed:12050338,
ECO:0000269|PubMed:15217993}.
/FTId=VAR_038973.
VARIANT 67 67 G -> R (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs387906523).
{ECO:0000269|PubMed:1734866}.
/FTId=VAR_007562.
VARIANT 67 67 G -> V (in AMYL-TTR; amyloid
polyneuropathy with carpal tunnel
syndrome).
/FTId=VAR_007563.
VARIANT 69 69 T -> A (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918081).
{ECO:0000269|PubMed:1301926,
ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:7655883}.
/FTId=VAR_007564.
VARIANT 69 69 T -> I (in AMYL-TTR).
{ECO:0000269|PubMed:10436378,
ECO:0000269|PubMed:17503405}.
/FTId=VAR_038974.
VARIANT 70 70 S -> I (in AMYL-TTR; amyloid
cardiomyopathy; dbSNP:rs121918080).
{ECO:0000269|PubMed:1520336}.
/FTId=VAR_007565.
VARIANT 70 70 S -> R (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs386134269).
{ECO:0000269|PubMed:10611950,
ECO:0000269|PubMed:23317988,
ECO:0000269|PubMed:2363717,
ECO:0000269|PubMed:7655883}.
/FTId=VAR_007566.
VARIANT 72 72 S -> P (in AMYL-TTR; amyloid
polyneuropathy).
/FTId=VAR_007567.
VARIANT 73 73 G -> E (in AMYL-TTR; dbSNP:rs121918097).
{ECO:0000269|PubMed:11445644}.
/FTId=VAR_038975.
VARIANT 74 74 E -> G (in AMYL-TTR; amyloid
polyneuropathy).
/FTId=VAR_007568.
VARIANT 74 74 E -> K (in AMYL-TTR; early-onset amyloid
polyneuropathy).
{ECO:0000269|PubMed:15214015}.
/FTId=VAR_038976.
VARIANT 75 75 L -> P (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918079).
{ECO:0000269|PubMed:1351039,
ECO:0000269|PubMed:16627944,
ECO:0000269|PubMed:7910950,
ECO:0000269|PubMed:9733771}.
/FTId=VAR_007569.
VARIANT 75 75 L -> Q (in AMYL-TTR).
{ECO:0000269|PubMed:12557757}.
/FTId=VAR_038977.
VARIANT 78 78 L -> H (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918069).
{ECO:0000269|PubMed:15217993}.
/FTId=VAR_007570.
VARIANT 78 78 L -> R (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918069).
{ECO:0000269|PubMed:1656975}.
/FTId=VAR_007571.
VARIANT 79 79 T -> K (in AMYL-TTR; amyloid
cardiomyopathy; dbSNP:rs730881163).
{ECO:0000269|PubMed:7850982}.
/FTId=VAR_007572.
VARIANT 80 80 T -> A (in AMYL-TTR; amyloid
polyneuropathy and cardiomyopathy;
dbSNP:rs121918070).
{ECO:0000269|PubMed:12050338,
ECO:0000269|PubMed:15217993,
ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:7655883}.
/FTId=VAR_007573.
VARIANT 81 81 E -> G (in AMYL-TTR).
{ECO:0000269|PubMed:17453626}.
/FTId=VAR_038978.
VARIANT 81 81 E -> K (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918086).
{ECO:0000269|PubMed:8352764}.
/FTId=VAR_007574.
VARIANT 84 84 F -> L (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918091).
{ECO:0000269|PubMed:11866053,
ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:2046936}.
/FTId=VAR_007575.
VARIANT 88 88 I -> L (in AMYL-TTR; amyloid
cardiomyopathy; dbSNP:rs121918085).
{ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:8038017}.
/FTId=VAR_007576.
VARIANT 89 89 Y -> H (in AMYL-TTR; leptomeningeal
amyloidosis; vitreous amyloid in some
patients; dbSNP:rs121918100).
{ECO:0000269|PubMed:12771253}.
/FTId=VAR_007577.
VARIANT 90 90 K -> N (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs267607160).
{ECO:0000269|PubMed:1436517}.
/FTId=VAR_007578.
VARIANT 91 91 V -> A (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918084).
{ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:8095302,
ECO:0000269|PubMed:8257997}.
/FTId=VAR_007579.
VARIANT 93 93 I -> V (in AMYL-TTR; amyloid
polyneuropathy).
{ECO:0000269|PubMed:10694917}.
/FTId=VAR_007580.
VARIANT 94 94 D -> H (in dbSNP:rs730881164).
/FTId=VAR_007581.
VARIANT 97 97 S -> Y (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918071).
{ECO:0000269|PubMed:15217993,
ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:2891727,
ECO:0000269|PubMed:7655883}.
/FTId=VAR_007582.
VARIANT 98 98 Y -> F (in AMYL-TTR).
{ECO:0000269|PubMed:16627944,
ECO:0000269|PubMed:17503405}.
/FTId=VAR_038979.
VARIANT 104 104 I -> N (in AMYL-TTR; vitrous amyloid).
{ECO:0000269|PubMed:17503405}.
/FTId=VAR_007583.
VARIANT 104 104 I -> S (in AMYL-TTR; amyloid
polyneuropathy; almost no RBP binding;
dbSNP:rs121918072).
{ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:3722385,
ECO:0000269|PubMed:8089102}.
/FTId=VAR_007584.
VARIANT 104 104 I -> T (in AMYL-TTR).
{ECO:0000269|PubMed:17503405}.
/FTId=VAR_038980.
VARIANT 109 109 E -> K (in AMYL-TTR; amyloid
polyneuropathy).
{ECO:0000269|PubMed:10842705}.
/FTId=VAR_010659.
VARIANT 109 109 E -> Q (in AMYL-TTR; amyloid
polyneuropathy and cardiomyopathy;
dbSNP:rs121918082).
{ECO:0000269|PubMed:1301926,
ECO:0000269|PubMed:7655883}.
/FTId=VAR_007585.
VARIANT 110 110 H -> N (in dbSNP:rs121918074).
{ECO:0000269|PubMed:1997217,
ECO:0000269|PubMed:7923855}.
/FTId=VAR_007586.
VARIANT 111 111 A -> S (in AMYL-TTR; amyloid
polyneuropathy).
{ECO:0000269|PubMed:10627135}.
/FTId=VAR_007587.
VARIANT 114 114 V -> A (in a patient with amyloidosis).
{ECO:0000269|PubMed:15217993,
ECO:0000269|PubMed:17503405}.
/FTId=VAR_038981.
VARIANT 117 117 A -> G (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918087).
{ECO:0000269|PubMed:10611950,
ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:8133316}.
/FTId=VAR_007588.
VARIANT 117 117 A -> S (in AMYL-TTR; dbSNP:rs267607161).
{ECO:0000269|PubMed:10611950}.
/FTId=VAR_038982.
VARIANT 121 121 G -> S (in dbSNP:rs755337715).
{ECO:0000269|PubMed:10671063,
ECO:0000269|PubMed:17503405}.
/FTId=VAR_007589.
VARIANT 122 122 P -> R.
/FTId=VAR_007590.
VARIANT 124 124 R -> C (in dbSNP:rs745834030).
/FTId=VAR_007591.
VARIANT 124 124 R -> H (in dbSNP:rs121918095).
{ECO:0000269|PubMed:10529370,
ECO:0000269|PubMed:15735344}.
/FTId=VAR_038983.
VARIANT 126 126 T -> N (in AMYL-TTR).
{ECO:0000269|PubMed:17503405}.
/FTId=VAR_038984.
VARIANT 127 127 I -> M (in AMYL-TTR).
{ECO:0000269|PubMed:17503405}.
/FTId=VAR_038985.
VARIANT 127 127 I -> V (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918089).
{ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:7914929,
ECO:0000269|PubMed:8081397}.
/FTId=VAR_007592.
VARIANT 129 129 A -> T (in DTTRH; increased affinity for
thyroxine; dbSNP:rs267607159).
{ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:1979335}.
/FTId=VAR_007593.
VARIANT 131 131 L -> M (in AMYL-TTR; dbSNP:rs121918073).
{ECO:0000269|PubMed:17503405}.
/FTId=VAR_007594.
VARIANT 134 134 Y -> C (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs121918075).
{ECO:0000269|PubMed:12403615,
ECO:0000269|PubMed:16185074,
ECO:0000269|PubMed:2161654}.
/FTId=VAR_007595.
VARIANT 134 134 Y -> H (in CTS1; amyloid deposit on
carpal tunnel; patients show no other
abnormalities; dbSNP:rs121918088).
{ECO:0000269|PubMed:8309582}.
/FTId=VAR_007598.
VARIANT 136 136 Y -> S (in AMYL-TTR; amyloid
polyneuropathy; dbSNP:rs730881167).
{ECO:0000269|PubMed:10627135}.
/FTId=VAR_007596.
VARIANT 136 136 Y -> V (requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:3675594}.
/FTId=VAR_007597.
VARIANT 139 139 T -> M (in Chicago variant;
dbSNP:rs28933981).
{ECO:0000269|PubMed:11866053,
ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:1877623}.
/FTId=VAR_007599.
VARIANT 140 140 A -> S (in AMYL-TTR; dbSNP:rs876658108).
{ECO:0000269|PubMed:12050338}.
/FTId=VAR_038986.
VARIANT 142 142 V -> A (in AMYL-TTR).
{ECO:0000269|PubMed:10211412}.
/FTId=VAR_038987.
VARIANT 142 142 V -> I (in AMYL-TTR; dbSNP:rs28933980).
{ECO:0000269|PubMed:12050338,
ECO:0000269|PubMed:17503405,
ECO:0000269|PubMed:3135807}.
/FTId=VAR_007600.
VARIANT 144 144 N -> S (in AMYL-TTR; dbSNP:rs144965179).
{ECO:0000269|PubMed:17577687}.
/FTId=VAR_038988.
MUTAGEN 107 107 F->M: Loss of tetramerization; when
associated with M-130.
{ECO:0000269|PubMed:11560492}.
MUTAGEN 130 130 L->M: Loss of tetramerization; when
associated with M-107.
{ECO:0000269|PubMed:11560492}.
CONFLICT 41 41 R -> P (in Ref. 3; AAA98771).
{ECO:0000305}.
CONFLICT 147 147 E -> D (in Ref. 12; CAG33189).
{ECO:0000305}.
TURN 23 26 {ECO:0000244|PDB:1TSH}.
STRAND 32 38 {ECO:0000244|PDB:1F86}.
TURN 39 42 {ECO:0000244|PDB:1F86}.
STRAND 49 55 {ECO:0000244|PDB:1F86}.
STRAND 57 59 {ECO:0000244|PDB:2B77}.
STRAND 61 68 {ECO:0000244|PDB:1F86}.
STRAND 73 75 {ECO:0000244|PDB:1F86}.
STRAND 77 80 {ECO:0000244|PDB:2QEL}.
TURN 81 83 {ECO:0000244|PDB:1F86}.
STRAND 86 93 {ECO:0000244|PDB:1F86}.
HELIX 95 101 {ECO:0000244|PDB:1F86}.
STRAND 107 118 {ECO:0000244|PDB:1F86}.
STRAND 120 122 {ECO:0000244|PDB:5JIM}.
STRAND 124 132 {ECO:0000244|PDB:1F86}.
STRAND 135 143 {ECO:0000244|PDB:1F86}.
SEQUENCE 147 AA; 15887 MW; 3A6AEBCBBA56BC44 CRC64;
MASHRLLLLC LAGLVFVSEA GPTGTGESKC PLMVKVLDAV RGSPAINVAV HVFRKAADDT
WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK ALGISPFHEH AEVVFTANDS
GPRRYTIAAL LSPYSYSTTA VVTNPKE


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