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Conantokin-G (Con-G) (CGX-1007) (Conotoxin GV) (Sleeper peptide)

 CKG_CONGE               Reviewed;         100 AA.
P07231; O61475;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
12-SEP-2018, entry version 108.
RecName: Full=Conantokin-G {ECO:0000303|PubMed:8999936};
Short=Con-G {ECO:0000303|PubMed:8999936};
AltName: Full=CGX-1007;
AltName: Full=Conotoxin GV {ECO:0000303|PubMed:6501296};
AltName: Full=Sleeper peptide {ECO:0000303|PubMed:6501296};
Flags: Precursor;
Conus geographus (Geography cone) (Nubecula geographus).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium.
NCBI_TaxID=6491;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-85.
TISSUE=Venom duct;
PubMed=9488665; DOI=10.1074/jbc.273.10.5447;
Bandyopadhyay P.K., Colledge C.J., Walker C.S., Zhou L.-M.,
Hillyard D.R., Olivera B.M.;
"Conantokin-G precursor and its role in gamma-carboxylation by a
vitamin K-dependent carboxylase from a Conus snail.";
J. Biol. Chem. 273:5447-5450(1998).
[2]
PROTEIN SEQUENCE OF 81-97, AMIDATION AT ASN-97,
GAMMA-CARBOXYGLUTAMATION AT GLU-83; GLU-84; GLU-87; GLU-90 AND GLU-94,
AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=6501296;
McIntosh J.M., Olivera B.M., Cruz L.J., Gray W.R.;
"Gamma-carboxyglutamate in a neuroactive toxin.";
J. Biol. Chem. 259:14343-14346(1984).
[3]
FUNCTION.
PubMed=2165278; DOI=10.1126/science.2165278;
Olivera B.M., Rivier J., Clark C., Ramilo C.A., Corpuz G.P.,
Abogadie F.C., Mena E.E., Woodward S.R., Hillyard D.R., Cruz L.J.;
"Diversity of Conus neuropeptides.";
Science 249:257-263(1990).
[4]
MUTAGENESIS OF LEU-85, AND SITE.
PubMed=11335724; DOI=10.1074/jbc.M102428200;
Klein R.C., Prorok M., Galdzicki Z., Castellino F.J.;
"The amino acid residue at sequence position 5 in the conantokin
peptides partially governs subunit-selective antagonism of recombinant
N-methyl-D-aspartate receptors.";
J. Biol. Chem. 276:26860-26867(2001).
[5]
METAL-BINDING SITES, AND COFACTOR.
PubMed=10406223; DOI=10.1034/j.1399-3011.1999.00042.x;
Blandl T., Warder S.E., Prorok M., Castellino F.J.;
"Binding of cations to individual gamma-carboxyglutamate residues of
conantokin-G and conantokin-T.";
J. Pept. Res. 53:453-464(1999).
[6]
THERAPEUTIC USAGE.
PubMed=12507705; DOI=10.1016/S0304-3959(02)00303-2;
Malmberg A.B., Gilbert H., McCabe R.T., Basbaum A.I.;
"Powerful antinociceptive effects of the cone snail venom-derived
subtype-selective NMDA receptor antagonists conantokins G and T.";
Pain 101:109-116(2003).
[7]
STRUCTURE BY NMR OF 81-97.
PubMed=9188685; DOI=10.1021/bi970321w;
Rigby A.C., Baleja J.D., Furie B.C., Furie B.;
"Three-dimensional structure of a gamma-carboxyglutamic acid-
containing conotoxin, conantokin G, from the marine snail Conus
geographus: the metal-free conformer.";
Biochemistry 36:6906-6914(1997).
[8]
STRUCTURE BY NMR OF 81-97.
PubMed=9398296; DOI=10.1021/bi9718550;
Rigby A.C., Baleja J.D., Li L., Pedersen L.G., Furie B.C., Furie B.;
"Role of gamma-carboxyglutamic acid in the calcium-induced structural
transition of conantokin G, a conotoxin from the marine snail Conus
geographus.";
Biochemistry 36:15677-15684(1997).
[9]
STRUCTURE BY NMR OF 81-97.
PubMed=8999936; DOI=10.1074/jbc.272.4.2291;
Skjaerbaek N., Nielsen K.J., Lewis R.J., Alewood P.F., Craik D.J.;
"Determination of the solution structures of conantokin-G and
conantokin-T by CD and NMR spectroscopy.";
J. Biol. Chem. 272:2291-2299(1997).
[10]
STRUCTURE BY NMR OF WILD-TYPE AND MUTANT CON-G, MUTAGENESIS OF GLN-89,
AND COFACTOR.
PubMed=26048991; DOI=10.1074/jbc.M115.650341;
Kunda S., Yuan Y., Balsara R.D., Zajicek J., Castellino F.J.;
"Hydroxyproline-induced helical disruption in conantokin Rl-B affects
subunit-selective antagonistic activities toward ion channels of N-
methyl-D-aspartate receptors.";
J. Biol. Chem. 290:18156-18172(2015).
-!- FUNCTION: Conantokins inhibit N-methyl-D-aspartate (NMDA)
receptors. This toxin is selective for the NR2B/GRIN2B subunit.
Induces sleep-like symptoms in young mice and hyperactivity in
older mice. {ECO:0000269|PubMed:2165278}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:10406223};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10406223,
ECO:0000269|PubMed:26048991};
Note=Divalent cations stabilize the toxin the in alpha-helix
conformation. {ECO:0000269|PubMed:10406223,
ECO:0000269|PubMed:26048991};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6501296}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
{ECO:0000305|PubMed:6501296}.
-!- PHARMACEUTICAL: Failed in phase II clinical trial. Was tested
under the name CGX-1007 by Cognetix Inc. to treat convulsion and
epilepsy.
-!- MISCELLANEOUS: The mutant Gln-89 consists of the addition of a
proline residue which is hydroxylated (4-hydroxyproline).
{ECO:0000269|PubMed:26048991}.
-!- MISCELLANEOUS: The mature peptide does not contain cysteine
residue. {ECO:0000305}.
-!- SIMILARITY: Belongs to the conotoxin B superfamily. {ECO:0000305}.
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EMBL; AF043141; AAC15669.1; -; mRNA.
PIR; A05168; A05168.
PDB; 1AD7; NMR; -; A=81-97.
PDB; 1AWY; NMR; -; A=81-97.
PDB; 1ONU; NMR; -; A=81-97.
PDB; 2DPQ; X-ray; 1.25 A; A=81-97.
PDB; 2MZL; NMR; -; A=81-97.
PDB; 2MZM; NMR; -; A=81-97.
PDBsum; 1AD7; -.
PDBsum; 1AWY; -.
PDBsum; 1ONU; -.
PDBsum; 2DPQ; -.
PDBsum; 2MZL; -.
PDBsum; 2MZM; -.
ProteinModelPortal; P07231; -.
SMR; P07231; -.
ConoServer; 1373; Conantokin-G precursor.
ConoServer; 1353; Conantokin-G precursor (variant).
EvolutionaryTrace; P07231; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0035792; C:other organism postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR005918; Conantokin_CS.
PROSITE; PS60025; CONANTOKIN; 1.
1: Evidence at protein level;
3D-structure; Amidation; Calcium; Cleavage on pair of basic residues;
Direct protein sequencing; Gamma-carboxyglutamic acid;
Ion channel impairing toxin; Ionotropic glutamate receptor inhibitor;
Magnesium; Metal-binding; Neurotoxin; Pharmaceutical;
Postsynaptic neurotoxin; Secreted; Signal; Toxin.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 80 {ECO:0000269|PubMed:6501296}.
/FTId=PRO_0000035060.
PEPTIDE 81 97 Conantokin-G.
{ECO:0000269|PubMed:6501296}.
/FTId=PRO_0000035061.
REGION 61 80 Gamma-carboxylation recognition sequence
that plays a role in the conversion of
Glu to carboxy-Glu (Gla). {ECO:0000305}.
METAL 83 83 Divalent metal cation; via 4-
carboxyglutamate.
{ECO:0000269|PubMed:10406223,
ECO:0000269|PubMed:26048991,
ECO:0000312|PDB:2DPQ}.
METAL 87 87 Divalent metal cation; via 4-
carboxyglutamate.
{ECO:0000269|PubMed:10406223,
ECO:0000269|PubMed:26048991,
ECO:0000312|PDB:2DPQ}.
METAL 90 90 Divalent metal cation; via 4-
carboxyglutamate.
{ECO:0000269|PubMed:10406223,
ECO:0000269|PubMed:26048991,
ECO:0000312|PDB:2DPQ}.
METAL 94 94 Divalent metal cation; via 4-
carboxyglutamate.
{ECO:0000269|PubMed:10406223,
ECO:0000269|PubMed:26048991}.
SITE 85 85 Important for selectivity.
MOD_RES 83 83 4-carboxyglutamate.
{ECO:0000269|PubMed:6501296}.
MOD_RES 84 84 4-carboxyglutamate.
{ECO:0000269|PubMed:6501296}.
MOD_RES 87 87 4-carboxyglutamate.
{ECO:0000269|PubMed:6501296}.
MOD_RES 90 90 4-carboxyglutamate.
{ECO:0000269|PubMed:6501296}.
MOD_RES 94 94 4-carboxyglutamate.
{ECO:0000269|PubMed:6501296}.
MOD_RES 97 97 Asparagine amide.
{ECO:0000269|PubMed:6501296}.
VARIANT 85 85 L -> V. {ECO:0000269|PubMed:9488665}.
MUTAGEN 85 85 L->I: No loss of inhibition of NR1a/NR2B
receptor; no inhibition of NR1a/NR2A
receptor (as for the wild-type).
{ECO:0000269|PubMed:11335724}.
MUTAGEN 85 85 L->V: No loss of inhibition of NR1a/NR2B
receptor; no inhibition of NR1a/NR2A
receptor (as for the wild-type).
{ECO:0000269|PubMed:11335724}.
MUTAGEN 85 85 L->Y: Little loss of inhibition of
NR1a/NR2B receptor; 70% of inhibition of
NR1a/NR2A receptor.
{ECO:0000269|PubMed:11335724}.
MUTAGEN 89 89 Q->QP: Loss of inhibition of NMDA
receptors from mouse cortical neurons
(the Pro is hydroxylated).
{ECO:0000269|PubMed:26048991,
ECO:0000312|PDB:2MZL}.
HELIX 82 96 {ECO:0000244|PDB:2DPQ}.
SEQUENCE 100 AA; 11267 MW; 3B0050FDFF2B9DFB CRC64;
MHLYTYLYLL VPLVTFHLIL GTGTLDDGGA LTERRSADAT ALKAEPVLLQ KSAARSTDDN
GKDRLTQMKR ILKQRGNKAR GEEELQENQE LIREKSNGKR


Related products :

Catalog number Product name Quantity
H-9960.0100 Conantokin G Salt _ Binding _ Synonym Conotoxin GV, Sleeper Peptide SumFormula C88H138N26O44 0.1 mg
H-9960.1000 Conantokin G Salt _ Binding _ Synonym Conotoxin GV, Sleeper Peptide SumFormula C88H138N26O44 1.0 mg
H-9960.0500 Conantokin G Salt _ Binding _ Synonym Conotoxin GV, Sleeper Peptide SumFormula C88H138N26O44 0.5 mg
orb71516 Conantokin G peptide This is Conantokin G peptide. For research use only. 1 mg
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orb71518 Conantokin T peptide This is Conantokin T peptide. For research use only. 1 mg
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
08CON012-00500 α-conotoxin MI (alpha conotoxin MI), α-conotoxin MI blocks nAChR 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
08CON012-01000 α-conotoxin MI (alpha conotoxin MI), α-conotoxin MI blocks nAChR 1000 ug
orb71185 [Glu3,4,7,10,14]-Conantokin G peptide This is [Glu3,4,7,10,14]-Conantokin G peptide. For research use only. 1 mg
08CON009-01000 Conantokin G, Conantokin G inhibits NMDA receptors 1000 ug
08CON009-00500 Conantokin G, Conantokin G inhibits NMDA receptors 500 ug
08CON001-00100 ω-Conotoxin MVIIA (omega conotoxin MVIIA), ω-Conotoxin MVIIA is a Cav2.2 channel blocker 100 ug
08CON001-00500 ω-Conotoxin MVIIA (omega conotoxin MVIIA), ω-Conotoxin MVIIA is a Cav2.2 channel blocker 500 ug
orb72044 alpha Conotoxin GI peptide This is alpha Conotoxin GI 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
orb71257 alpha Conotoxin EI peptide This is alpha Conotoxin EI peptide. For research use only. 1 mg
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orb70283 alpha Conotoxin SI peptide This is alpha Conotoxin SI peptide. For research use only. 1 mg
orb71260 alpha Conotoxin SIA peptide This is alpha Conotoxin SIA peptide. For research use only. 1 mg
orb71259 alpha Conotoxin MI peptide This is alpha Conotoxin MI peptide. For research use only. 1 mg
08CON003-00500 ω-conotoxin GVIA, ω-conotoxin GVIA blocks Cav2.2 500 ug


 

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