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1awy

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NMR STRUCTURE OF CALCIUM BOUND CONFORMER OF CONANTOKIN G, MINIMIZED AVERAGE STRUCTURE

Structural highlights

1awy is a 1 chain structure with sequence from Conus geographus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CKG_CONGE 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.^[1]

Publication Abstract from PubMed

Conantokin G is a gamma-carboxyglutamic acid- (Gla-) containing conotoxin isolated from the venom of the marine cone snail Conus geographus. This 17-residue polypeptide, which contains five gamma-carboxyglutamic acid residues, is a N-methyl-d-aspartate- (NMDA-) type glutamate receptor antagonist. To investigate the role of gamma-carboxyglutamic acid in the calcium-induced structural transition of conantokin G, we determined the three-dimensional structure of the conantokin G/Ca2+ complex by two-dimensional 1H NMR spectroscopy and compared it to the high-resolution structure of conantokin G in the absence of metal ions [Rigby et al. (1997) Biochemistry 36, 6906]. Complete resonance assignments were made by two dimensional 1H NMR spectroscopy at pH 5.6 in the presence of saturating amounts of Ca2+. Distance geometry and simulated annealing methods were used to derive 23 convergent structures from a set of 302 interproton distance restraints and two torsion angle measurements. A high-resolution structure, with the backbone root mean square deviation to the geometric average of the 23 structures of 0.6 +/- 0.1 A, contains a linear alpha-helix from Gla 3 to Lys 15. Gla residues 3, 7, 10, and 14 are aligned in a linear array on one face of the helix. A genetic algorithm was applied to determine the calcium positions in conantokin G, and the conantokin G/Ca2+ complex refined by molecular simulation. Upon binding of Ca2+ to gamma-carboxyglutamic acid, conantokin G undergoes a conformational transition from a distorted curvilinear 310 helix to a linear alpha-helix. Occupancy of the metal binding sites, defined by gamma-carboxyglutamic acids, results in formation of a calcium-carboxylate network that linearizes the helix and exposes the hydrophobic amino acids on the opposite face of the helix.

Role of gamma-carboxyglutamic acid in the calcium-induced structural transition of conantokin G, a conotoxin from the marine snail Conus geographus.,Rigby AC, Baleja JD, Li L, Pedersen LG, Furie BC, Furie B Biochemistry. 1997 Dec 16;36(50):15677-84. PMID:9398296^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Olivera BM, Rivier J, Clark C, Ramilo CA, Corpuz GP, Abogadie FC, Mena EE, Woodward SR, Hillyard DR, Cruz LJ. Diversity of Conus neuropeptides. Science. 1990 Jul 20;249(4966):257-63. PMID:2165278
↑ Rigby AC, Baleja JD, Li L, Pedersen LG, Furie BC, 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. 1997 Dec 16;36(50):15677-84. PMID:9398296 doi:10.1021/bi9718550

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1awy"

@@ Line 1: / Line 1: @@
 ==NMR STRUCTURE OF CALCIUM BOUND CONFORMER OF CONANTOKIN G, MINIMIZED AVERAGE STRUCTURE==
-<StructureSection load='1awy' size='340' side='right' caption='[[1awy]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1awy' size='340' side='right'caption='[[1awy]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1awy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Conus_geographus Conus geographus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AWY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1awy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_geographus Conus geographus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AWY FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1awy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1awy RCSB], [http://www.ebi.ac.uk/pdbsum/1awy PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1awy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awy OCA], [https://pdbe.org/1awy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1awy RCSB], [https://www.ebi.ac.uk/pdbsum/1awy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1awy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CXKG_CONGE CXKG_CONGE]] 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.<ref>PMID:2165278</ref>
+[https://www.uniprot.org/uniprot/CKG_CONGE CKG_CONGE] 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.<ref>PMID:2165278</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1awy" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 21: / Line 24: @@
 </StructureSection>
 [[Category: Conus geographus]]
-[[Category: Baleja, J D]]
+[[Category: Large Structures]]
-[[Category: Furie, B]]
+[[Category: Baleja JD]]
-[[Category: Furie, B C]]
+[[Category: Furie B]]
-[[Category: Leping, L]]
+[[Category: Furie BC]]
-[[Category: Pedersen, L G]]
+[[Category: Leping L]]
-[[Category: Rigby, A C]]
+[[Category: Pedersen LG]]
-[[Category: Calcium bound]]
+[[Category: Rigby AC]]
-[[Category: Conantokin g]]
-[[Category: Conotoxin]]
-[[Category: Gamma-carboxyglutamic acid]]
-[[Category: Venom]]

1awy

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Current revision

NMR STRUCTURE OF CALCIUM BOUND CONFORMER OF CONANTOKIN G, MINIMIZED AVERAGE STRUCTURE

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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