Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Mu-conotoxin GVIIJ (Conotoxin muO-GVIIJ) (G086) (G19) (MuO'section sign'-GVIIJ)

 CO17J_CONGE             Reviewed;          82 AA.
X5IWS1;
15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
15-FEB-2017, sequence version 2.
22-NOV-2017, entry version 15.
RecName: Full=Mu-conotoxin GVIIJ {ECO:0000303|PubMed:26817840};
AltName: Full=Conotoxin muO-GVIIJ {ECO:0000303|PubMed:26817840};
AltName: Full=G086 {ECO:0000303|PubMed:24662800};
AltName: Full=G19 {ECO:0000303|PubMed:22742208};
AltName: Full=MuO'section sign'-GVIIJ {ECO:0000303|PubMed:26817840};
Flags: Precursor;
Conus geographus (Geography cone) (Nubecula geographus).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus.
NCBI_TaxID=6491;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom duct;
PubMed=22742208; DOI=10.1186/1471-2164-13-284;
Hu H., Bandyopadhyay P.K., Olivera B.M., Yandell M.;
"Elucidation of the molecular envenomation strategy of the cone snail
Conus geographus through transcriptome sequencing of its venom duct.";
BMC Genomics 13:284-284(2012).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-75, PROTEIN SEQUENCE OF 48-59 AND
65-74, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
TISSUE=Venom, and Venom duct;
PubMed=24662800; DOI=10.1038/ncomms4521;
Dutertre S., Jin A.-H., Vetter I., Hamilton B., Sunagar K.,
Lavergne V., Dutertre V., Fry B.G., Antunes A., Venter D.J.,
Alewood P.F., Lewis R.J.;
"Evolution of separate predation- and defence-evoked venoms in
carnivorous cone snails.";
Nat. Commun. 5:3521-3521(2014).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-82, FUNCTION,
SYNTHESIS OF 48-82, DISULFIDE BOND, BROMINATION AT TRP-49,
HYDROXYLATION AT PRO-53, S-CYSTEINYLATION AT CYS-71, AND MASS
SPECTROMETRY.
TISSUE=Venom, and Venom duct;
PubMed=24497506; DOI=10.1073/pnas.1324189111;
Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G.,
Wickenden A.D., Olivera B.M., Yoshikami D., Zhang M.M.;
"A disulfide tether stabilizes the block of sodium channels by the
conotoxin muO[section sign]-GVIIJ.";
Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
[4]
SYNTHESIS OF 48-82 (WITHOUT BROMINATION).
PubMed=26039939; DOI=10.1021/acs.biochem.5b00390;
Zhang M.M., Gajewiak J., Azam L., Bulaj G., Olivera B.M.,
Yoshikami D.;
"Probing the redox states of sodium channel cysteines at the binding
site of muO[section sign]-conotoxin GVIIJ.";
Biochemistry 54:3911-3920(2015).
[5]
STRUCTURE BY NMR OF 48-82 OF MUTANT CYS-71, SYNTHESIS OF 48-82
(WITHOUT BROMINATION), FUNCTION, DISULFIDE BONDS, AND MUTAGENESIS OF
TRP-49; TRP-49; ASP-52; PRO-53; THR-56; LYS-59; LEU-60; ARG-61;
LEU-62; TYR-63; SER-66; PHE-68; ASP-70; TYR-72; THR-73; LYS-74;
THR-75; LYS-77; ASP-78 AND LYS-79.
PubMed=26817840; DOI=10.1074/jbc.M115.697672;
Green B.R., Gajewiak J., Chhabra S., Skalicky J.J., Zhang M.,
Rivier J.E., Bulaj G., Olivera B.M., Yoshikami D., Norton R.S.;
"Structural basis for the inhibition of voltage-gated sodium channels
by conotoxin muO-GVIIJ.";
J. Biol. Chem. 291:7205-7220(2016).
-!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav).
This toxin (GVIIJ(SSG)) blocks Nav1.1/SCN1A (Kd=11 nM),
Nav1.2/SCN2A (Kd=11 nM), Nav1.3/SCN3A (Kd=15 nM), Nav1.4/SCN4A
(Kd=4.7 nM), Nav1.6/SCN8A (Kd=360 nM) and Nav1.7/SCN9A (Kd=41 nM)
(PubMed:24497506, PubMed:26039939). It binds the channel at the
newly described site 8, which is composed by two surfaces whose
one contains a non-disulfide-bonded cysteine (which is free to
covalently bind the toxin Cys-71) (PubMed:24497506). It is
noteworthy that coexpression of subunits beta-2 or beta-4 (but not
beta-1 or beta-3) protects rNav1.1-1.7 against block by the toxin,
since these subunits (thanks to their extracellular domain)
covalently bind to the key cysteine of the channel, thus
preventing the covalent binding of the toxin (PubMed:24497506).
{ECO:0000269|PubMed:24497506, ECO:0000269|PubMed:26039939,
ECO:0000269|PubMed:26817840}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24662800}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
{ECO:0000305|PubMed:22742208}.
-!- DOMAIN: The presence of a 'disulfide through disulfide knot'
structurally defines this protein as a knottin.
{ECO:0000269|PubMed:26817840}.
-!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
{ECO:0000305}.
-!- PTM: Cys-71 is a key residue that tethers to the channel by
covalent attachment, leading to nearly irreversible inhibition
(k(off) very low) (PubMed:24497506, PubMed:26817840). In order to
determine the solution structure without dimerization, this
residue was mutated to Cys. {ECO:0000269|PubMed:24497506,
ECO:0000269|PubMed:26817840}.
-!- MASS SPECTROMETRY: Mass=3934.49; Method=MALDI; Range=48-82;
Evidence={ECO:0000269|PubMed:24497506};
-!- MISCELLANEOUS: This toxin shows a very low affinity to
Nav1.5/SCN5A (Kd=207 uM) and does not show activity on
rNav1.8/SCN10A. {ECO:0000269|PubMed:24497506}.
-!- SIMILARITY: Belongs to the conotoxin O1 superfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAO65619.1; Type=Erroneous termination; Positions=76; Note=Translated as Cys.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
Note=synthetic GVIIJ[C71S];
URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=26674";
-!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
Note=synthetic GVIIJ disulfide-linked with cysteamine;
URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=26675";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB910851; BAO65619.1; ALT_SEQ; mRNA.
PDB; 2N8H; NMR; -; A=48-82.
PDBsum; 2N8H; -.
SMR; X5IWS1; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR004214; Conotoxin.
Pfam; PF02950; Conotoxin; 1.
1: Evidence at protein level;
3D-structure; Bromination; Direct protein sequencing; Disulfide bond;
Hydroxylation; Ion channel impairing toxin; Knottin; Secreted; Signal;
Toxin; Voltage-gated sodium channel impairing toxin.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 47 {ECO:0000269|PubMed:24497506}.
/FTId=PRO_0000438880.
CHAIN 48 82 Mu-conotoxin GVIIJ.
{ECO:0000269|PubMed:24497506}.
/FTId=PRO_5004957961.
SITE 59 59 Functionally important residue, that
binds to the site 8 of the channel.
{ECO:0000305|PubMed:26817840}.
SITE 61 61 Functionally important residue, that
binds to the site 8 of the channel.
{ECO:0000305|PubMed:26817840}.
SITE 63 63 Functionally important residue, that
binds to the site 8 of the channel.
{ECO:0000305|PubMed:26817840}.
SITE 71 71 Functionally important residue, that
binds to the site 8 of the channel
(distinct surface that K-59; R-61 and Y-
63). {ECO:0000305|PubMed:26817840}.
MOD_RES 49 49 6'-bromotryptophan.
{ECO:0000269|PubMed:24497506}.
MOD_RES 53 53 4-hydroxyproline.
{ECO:0000269|PubMed:24497506}.
MOD_RES 71 71 S-cysteinyl cysteine.
{ECO:0000269|PubMed:24497506}.
DISULFID 50 65 {ECO:0000244|PDB:2N8H,
ECO:0000269|PubMed:24497506,
ECO:0000269|PubMed:26817840}.
DISULFID 57 69 {ECO:0000244|PDB:2N8H,
ECO:0000269|PubMed:24497506,
ECO:0000269|PubMed:26817840}.
DISULFID 65 76 {ECO:0000244|PDB:2N8H,
ECO:0000269|PubMed:24497506,
ECO:0000269|PubMed:26817840}.
MUTAGEN 49 49 W->A: 10-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 52 52 D->K: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 53 53 P->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 56 56 T->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 59 59 K->D: 280-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 60 60 L->A: Small decrease in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 61 61 R->D: 133-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 62 62 L->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 63 63 Y->A: 53-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 66 66 S->A: Small decrease in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 68 68 F->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 70 70 D->N: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 72 72 Y->A,D,R: No change or small decrease in
affinity to Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 73 73 T->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 74 74 K->D: 13-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 74 74 K->G,F: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 75 75 T->A: Small decrease in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 77 77 K->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 78 78 D->K: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 79 79 K->D: Small decrease in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
STRAND 58 61 {ECO:0000244|PDB:2N8H}.
STRAND 64 67 {ECO:0000244|PDB:2N8H}.
TURN 71 74 {ECO:0000244|PDB:2N8H}.
SEQUENCE 82 AA; 8871 MW; D8A907002C69A971 CRC64;
MKLTCVVIVA ALLLTACQLI TALDCGGTQK HRALRSTIKL SLLRQHRGWC GDPGATCGKL
RLYCCSGFCD CYTKTCKDKS SA


Related products :

Catalog number Product name Quantity
08CON015-01000 α-conotoxin GI (alpha conotoxin GI), α-conotoxin G blocks nAChR receptors 1000 ug
08CON015-00500 α-conotoxin GI (alpha conotoxin GI), α-conotoxin G blocks nAChR receptors 500 ug
08CON011-01000 α-conotoxin IMI (alpha conotoxin IMI), α-conotoxin IMI blocks nAChR 1000 ug
08CON011-00500 α-conotoxin IMI (alpha conotoxin IMI), α-conotoxin IMI blocks nAChR 500 ug
08CON012-00500 α-conotoxin MI (alpha conotoxin MI), α-conotoxin MI blocks nAChR 500 ug
08CON012-01000 α-conotoxin MI (alpha conotoxin MI), α-conotoxin MI blocks nAChR 1000 ug
08CON001-00500 ω-Conotoxin MVIIA (omega conotoxin MVIIA), ω-Conotoxin MVIIA is a Cav2.2 channel blocker 500 ug
08CON001-00100 ω-Conotoxin MVIIA (omega conotoxin MVIIA), ω-Conotoxin MVIIA is a Cav2.2 channel blocker 100 ug
08CON003-00500 ω-conotoxin GVIA, ω-conotoxin GVIA blocks Cav2.2 500 ug
08CON003-01000 ω-conotoxin GVIA, ω-conotoxin GVIA blocks Cav2.2 1000 ug
08CON003-00100 ω-conotoxin GVIA, ω-conotoxin GVIA blocks Cav2.2 100 ug
08CON002-01000 ω-conotoxin MVIIC (omega contoxin MVIIC), ω-conotoxin MVIIC is a calcium channel blocker 1000 ug
08CON002-00500 ω-conotoxin MVIIC (omega contoxin MVIIC), ω-conotoxin MVIIC is a calcium channel blocker 500 ug
08CON002-00100 ω-conotoxin MVIIC (omega contoxin MVIIC), ω-conotoxin MVIIC is a calcium channel blocker 100 ug
08CON006-00100 μ-Conotoxin PIIIA, μ-Conotoxin PIIIA blocks Nav1.2 and Nav1.7 channels 100 ug
08CON006-00500 μ-Conotoxin PIIIA, μ-Conotoxin PIIIA blocks Nav1.2 and Nav1.7 channels 500 ug
orb72044 alpha Conotoxin GI peptide This is alpha Conotoxin GI peptide. For research use only. 0.5 mg
orb71260 alpha Conotoxin SIA peptide This is alpha Conotoxin SIA peptide. For research use only. 1 mg
orb70283 alpha Conotoxin SI peptide This is alpha Conotoxin SI peptide. For research use only. 1 mg
orb71257 alpha Conotoxin EI peptide This is alpha Conotoxin EI peptide. For research use only. 1 mg
orb71259 alpha Conotoxin MI peptide This is alpha Conotoxin MI peptide. For research use only. 1 mg
orb72045 alpha Conotoxin IMI peptide This is alpha Conotoxin IMI peptide. For research use only. 0.5 mg
orb71258 alpha Conotoxin GS peptide This is alpha Conotoxin GS peptide. For research use only. 1 mg
ST14-1 Conotoxin mI 1 mg
ST14-500 Conotoxin mI 500 µg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur