View source for 1b45


==ALPHA-CNIA CONOTOXIN FROM CONUS CONSORS, NMR, 43 STRUCTURES==
<StructureSection load='1b45' size='340' side='right'caption='[[1b45]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1b45]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_consors Conus consors]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B45 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 43 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=1b45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b45 OCA], [https://pdbe.org/1b45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b45 RCSB], [https://www.ebi.ac.uk/pdbsum/1b45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b45 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CA1A_CONCN CA1A_CONCN] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. CnIA and CnIB block muscular nAChR alpha-1/gamma and alpha-1/delta subunits.
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== Publication Abstract from PubMed ==
Two novel alpha-conotoxins were purified and characterized from the venom of the fish-hunting cone snail Conus consors. These peptides were identified by screening HPLC fractions of the crude venom and by binding experiments with Torpedo nicotinic acetylcholine receptor. The toxins named alpha-CnIA and alpha-CnIB exhibited sequences of 14 and 12 amino acids, respectively. The alpha-CnIA represents the main alpha-conotoxin contained in the venom, whereas alpha-CnIB is present in a relatively small amount. Chemical synthesis of alpha-CnIA was carried out using the Fmoc methodology by selective disulfide bond formation. The biological activity of the toxin was assessed in fish and mice. The alpha-CnIA inhibited the fixation of iodinated alpha-bungarotoxin to Torpedo nicotinic acetylcholine receptors with an IC50 of 0.19 microM which can be compared to the IC50 of 0.31 microM found for the previously characterized alpha-MI isolated from the piscivorous Conus magus. The synthetic alpha-CnIA blocked spontaneous and evoked synaptic potentials in frog and mouse isolated neuromuscular preparations at sub-micromolar concentrations. Solution NMR of this toxin indicated a conformational heterogeneity with the existence of different conformers in solution, at slow and intermediate exchange rates relative to the NMR chemical shift time scale, similar to that reported for alpha-GI and alpha-MI. NMR structures were calculated for the major NMR signals representing more than 80% of the population at 5 degrees C.

Biochemical characterization and nuclear magnetic resonance structure of novel alpha-conotoxins isolated from the venom of Conus consors.,Favreau P, Krimm I, Le Gall F, Bobenrieth MJ, Lamthanh H, Bouet F, Servent D, Molgo J, Menez A, Letourneux Y, Lancelin JM Biochemistry. 1999 May 11;38(19):6317-26. PMID:10320362<ref>PMID:10320362</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Conus consors]]
[[Category: Large Structures]]
[[Category: Bobenrieth MJ]]
[[Category: Bouet F]]
[[Category: Favreau P]]
[[Category: Krimm I]]
[[Category: Lamthanh H]]
[[Category: Lancelin JM]]
[[Category: Le Gall F]]
[[Category: Letourneux Y]]
[[Category: Menez A]]
[[Category: Molgo J]]
[[Category: Servent D]]