1not: Difference between revisions
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==THE 1.2 ANGSTROM STRUCTURE OF G1 ALPHA CONOTOXIN== | |||
<StructureSection load='1not' size='340' side='right'caption='[[1not]], [[Resolution|resolution]] 1.20Å' scene=''> | |||
| | == Structural highlights == | ||
<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='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='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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAIA_CONGE CAIA_CONGE] | |||
<div style="background-color:#fffaf0;"> | |||
== | == 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. | 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<ref>PMID:8784187</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1not" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Conus geographus]] | [[Category: Conus geographus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Edmundson | [[Category: Edmundson AB]] | ||
[[Category: Gray | [[Category: Gray WR]] | ||
[[Category: Guddat | [[Category: Guddat LW]] | ||
[[Category: Martin | [[Category: Martin JL]] | ||
[[Category: Shan | [[Category: Shan L]] | ||
Latest revision as of 05:32, 5 June 2024
THE 1.2 ANGSTROM STRUCTURE OF G1 ALPHA CONOTOXIN
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