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New page: left|200px<br /><applet load="1ul2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ul2" /> '''Solution Conformation of alpha-Conotoxin GIC...
 
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[[Image:1ul2.jpg|left|200px]]<br /><applet load="1ul2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ul2" />
'''Solution Conformation of alpha-Conotoxin GIC'''<br />


==Overview==
==Solution Conformation of alpha-Conotoxin GIC==
Alpha-conotoxin GIC is a 16-residue peptide isolated from the venom of the, cone snail Conus geographus. Alpha-conotoxin GIC potently blocks the, alpha3beta2 subtype of human nicotinic acetylcholine receptor, showing a, high selectivity for neuronal versus muscle subtype [McIntosh, Dowell, Watkins, Garrett, Yoshikami, and Olivera (2002) J. Biol. Chem. 277, 33610-33615]. We have now determined the three-dimensional solution, structure of alpha-conotoxin GIC by NMR spectroscopy. The structure of, alpha-conotoxin GIC is well defined with backbone and heavy atom root mean, square deviations (residues 2-16) of 0.53 A and 0.96 A respectively., Structure and surface comparison of alpha-conotoxin GIC with the other, alpha4/7 subfamily conotoxins reveals unique structural aspects of, alpha-conotoxin GIC. In particular, the structural comparison between, alpha-conotoxins GIC and MII indicates molecular features that may confer, their similar receptor specificity profile, as well as those that provide, the unique binding characteristics of alpha-conotoxin GIC.
<StructureSection load='1ul2' size='340' side='right'caption='[[1ul2]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ul2]] 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=1UL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UL2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1ul2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ul2 OCA], [https://pdbe.org/1ul2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ul2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ul2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ul2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CA1C_CONGE CA1C_CONGE] Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin reversibly blocks neuronal nAChRs (alpha-3/beta-2 = alpha-6 or -3/beta-2 or -3 > alpha-3/beta-4 = alpha-4/beta-2).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Alpha-conotoxin GIC is a 16-residue peptide isolated from the venom of the cone snail Conus geographus. Alpha-conotoxin GIC potently blocks the alpha3beta2 subtype of human nicotinic acetylcholine receptor, showing a high selectivity for neuronal versus muscle subtype [McIntosh, Dowell, Watkins, Garrett, Yoshikami, and Olivera (2002) J. Biol. Chem. 277, 33610-33615]. We have now determined the three-dimensional solution structure of alpha-conotoxin GIC by NMR spectroscopy. The structure of alpha-conotoxin GIC is well defined with backbone and heavy atom root mean square deviations (residues 2-16) of 0.53 A and 0.96 A respectively. Structure and surface comparison of alpha-conotoxin GIC with the other alpha4/7 subfamily conotoxins reveals unique structural aspects of alpha-conotoxin GIC. In particular, the structural comparison between alpha-conotoxins GIC and MII indicates molecular features that may confer their similar receptor specificity profile, as well as those that provide the unique binding characteristics of alpha-conotoxin GIC.


==About this Structure==
Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors.,Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH Biochem J. 2004 Jun 1;380(Pt 2):347-52. PMID:14992691<ref>PMID:14992691</ref>
1UL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UL2 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem J. 2004 Jun 1;380(Pt 2):347-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14992691 14992691]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1ul2" style="background-color:#fffaf0;"></div>
[[Category: Chi, S.W.]]
== References ==
[[Category: Han, K.H.]]
<references/>
[[Category: Kim, D.H.]]
__TOC__
[[Category: McIntosh, J.M.]]
</StructureSection>
[[Category: Olivera, B.M.]]
[[Category: Conus geographus]]
[[Category: NH2]]
[[Category: Large Structures]]
[[Category: alpha-helix]]
[[Category: Chi S-W]]
[[Category: beta-turn]]
[[Category: Han K-H]]
[[Category: c-terminal amidation]]
[[Category: Kim D-H]]
[[Category: two disulfide bonds]]
[[Category: McIntosh JM]]
 
[[Category: Olivera BM]]
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