1zlc
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(New page: 200px<br /><applet load="1zlc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zlc" /> '''Solution Conformation of alpha-conotoxin PIA...)
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Revision as of 05:23, 21 November 2007
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Solution Conformation of alpha-conotoxin PIA
Overview
alpha-Conotoxin PIA is a novel nicotinic acetylcholine receptor (nAChR), antagonist isolated from Conus purpurascens that targets nAChR subtypes, containing alpha6 and alpha3 subunits. alpha-conotoxin PIA displays, 75-fold higher affinity for rat alpha6/alpha3beta2beta3 nAChRs than for, rat alpha3beta2 nAChRs. We have determined the three-dimensional structure, of alpha-conotoxin PIA by nuclear magnetic resonance spectroscopy. The, alpha-conotoxin PIA has an "omega-shaped" overall topology as other, alpha4/7 subfamily conotoxins. Yet, unlike other neuronally targeted, alpha4/7-conotoxins, its N-terminal tail Arg1-Asp2-Pro3 protrudes out of, its main molecular body because Asp2-Pro3-Cys4-Cys5 forms a stable type I, beta-turn. In addition, a kink introduced by Pro15 in the second loop of, this toxin provides a distinct steric and electrostatic environment from, those in alpha-conotoxins MII and GIC. By comparing the structure of, alpha-conotoxin PIA with other functionally related alpha-conotoxins we, suggest structural features in alpha-conotoxin PIA that may be associated, with its unique receptor recognition profile.
About this Structure
1ZLC is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of alpha-conotoxin PIA, a novel antagonist of alpha6 subunit containing nicotinic acetylcholine receptors., Chi SW, Lee SH, Kim DH, Kim JS, Olivera BM, McIntosh JM, Han KH, Biochem Biophys Res Commun. 2005 Dec 30;338(4):1990-7. Epub 2005 Nov 7. PMID:16289101
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