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| | <StructureSection load='1not' size='340' side='right'caption='[[1not]], [[Resolution|resolution]] 1.20Å' scene=''> | | <StructureSection load='1not' size='340' side='right'caption='[[1not]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1not]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Conge Conge]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NOT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1not]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_geographus Conus geographus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NOT FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</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=1not FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1not OCA], [http://pdbe.org/1not PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1not RCSB], [http://www.ebi.ac.uk/pdbsum/1not PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1not ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1not FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1not OCA], [https://pdbe.org/1not PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1not RCSB], [https://www.ebi.ac.uk/pdbsum/1not PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1not ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CA1A_CONGE CA1A_CONGE]] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. The higher affinity site for alpha-conotoxin GI is the alpha/delta site on mouse muscle-derived BC3H-1 receptor, and the other site (alpha/gamma site) on nicotinic receptors from Torpedo californica electric organ. | + | [https://www.uniprot.org/uniprot/CAIA_CONGE CAIA_CONGE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Conge]] | + | [[Category: Conus geographus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Edmundson, A B]] | + | [[Category: Edmundson AB]] |
| - | [[Category: Gray, W R]] | + | [[Category: Gray WR]] |
| - | [[Category: Guddat, L W]] | + | [[Category: Guddat LW]] |
| - | [[Category: Martin, J L]] | + | [[Category: Martin JL]] |
| - | [[Category: Shan, L]] | + | [[Category: Shan L]] |
| - | [[Category: Acetylcholine receptor]]
| + | |
| - | [[Category: Conotoxin]]
| + | |
| - | [[Category: Disulphide loop]]
| + | |
| - | [[Category: Venom]]
| + | |
| Structural highlights
Function
CAIA_CONGE
Publication Abstract from PubMed
Predatory marine snails of the genus Conus paralyze their fish prey by injecting a potent toxin. The alpha-conotoxin GI is a 13-residue peptide isolated from venom of Conus geographus. It functions by blocking the postsynaptic nicotinic acetylcholine receptor. After crystallization in deionized water, the three-dimensional structure of the GI neurotoxin was determined to 1.2 A resolution by X-ray crystallography. This structure, which can be described as a triangular slab, shows overall similarities to those derived by NMR, CD, and predictive methods. The principal framework of the molecule is provided by two disulfide bonds, one linking Cys 2 and Cys 7 and the other Cys 3 and Cys 13. Opposite ends of the sequence are drawn together even further by hydrogen bonds between Glu 1 and Cys 13 and between Cys 2 and Ser 12. Since the C-terminus is amidated, only one negative charge is present (carboxylate of Glu 1), and this is not implicated in receptor binding. Two positively charged regions (the alpha-amino group of Glu 1 and the guanido group of Arg 9) are situated 15 A apart at the corners of the triangular face of the molecule. phi, psi angles characteristic of a 3(10) helix were observed for residues 5-7. For residues 8-11, these angles were consistent with either a type I beta-turn or a distorted 3(10) helix.
Three-dimensional structure of the alpha-conotoxin GI at 1.2 A resolution.,Guddat LW, Martin JA, Shan L, Edmundson AB, Gray WR Biochemistry. 1996 Sep 3;35(35):11329-35. PMID:8784187[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guddat LW, Martin JA, Shan L, Edmundson AB, Gray WR. Three-dimensional structure of the alpha-conotoxin GI at 1.2 A resolution. Biochemistry. 1996 Sep 3;35(35):11329-35. PMID:8784187 doi:http://dx.doi.org/10.1021/bi960820h
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