2gcz
From Proteopedia
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Solution Structure of alpha-Conotoxin OmIA
Overview
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.
About this Structure
2GCZ is a Protein complex structure of sequences from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
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
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