View source for 2gcz


==Solution Structure of alpha-Conotoxin OmIA==
<StructureSection load='2gcz' size='340' side='right'caption='[[2gcz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gcz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_omaria Conus omaria]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GCZ 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=2gcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gcz OCA], [https://pdbe.org/2gcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gcz RCSB], [https://www.ebi.ac.uk/pdbsum/2gcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gcz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CA1A_CONOM CA1A_CONOM] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks alpha-3/beta-2 (IC(50)=11 nM), alpha-7 (IC(50)=27.1) and alpha-6/alpha-3-beta-2-beta-3 (IC(50)=201 nM) subunits of nAChR.<ref>PMID:16803900</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
alpha-Conotoxin OmIA from Conus omaria is the only alpha-conotoxin that shows a approximately 20-fold higher affinity to the alpha3beta2 over the alpha6beta2 subtype of nicotinic acetylcholine receptor. We have determined a three-dimensional structure of alpha-conotoxin OmIA by nuclear magnetic resonance spectroscopy. alpha-Conotoxin OmIA has an "omega-shaped" overall topology with His(5)-Asn(12) forming an alpha-helix. Structural features of alpha-conotoxin OmIA responsible for its selectivity are suggested by comparing its surface characteristics with other functionally related alpha4/7 subfamily conotoxins. Reduced size of the hydrophilic area in alpha-conotoxin OmIA seems to be associated with the reduced affinity towards the alpha6beta2 nAChR subtype.

Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist alpha-conotoxin OmIA that discriminates alpha3 vs. alpha6 nAChR subtypes.,Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH Biochem Biophys Res Commun. 2006 Jun 23;345(1):248-54. Epub 2006 Apr 27. PMID:16678128<ref>PMID:16678128</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2gcz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Conus omaria]]
[[Category: Large Structures]]
[[Category: Chi S-W]]
[[Category: Han K-H]]
[[Category: Kim D-H]]
[[Category: McIntosh JM]]
[[Category: Olivera BM]]