2i28
From Proteopedia
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Solution Structure of alpha-Conotoxin BuIA
Overview
We have determined a high-resolution three-dimensional structure of, alpha-conotoxin BuIA, a 13-residue peptide toxin isolated from Conus, bullatus. Despite its unusual 4/4 disulfide bond layout alpha-conotoxin, BuIA exhibits strong antagonistic activity at alpha6/alpha3beta2beta3, alpha3beta2, and alpha3beta4 nAChR subtypes like some alpha4/7 conotoxins., alpha-Conotoxin BuIA lacks the C-terminal beta-turn present within the, second disulfide loop of alpha4/7 conotoxins, having only a "pseudo, omega-shaped" molecular topology. Nevertheless, it contains a functionally, critical two-turn helix motif, a feature ubiquitously found in alpha4/7, conotoxins. Such an aspect seems mainly responsible for similarities in, the receptor recognition profile of alpha-conotoxin BuIA to alpha4/7, conotoxins. Structural comparison of alpha-conotoxin BuIA with alpha4/7, conotoxins and alpha4/3 conotoxin ImI suggests that presence of the second, helical turn portion of the two-turn helix motif in alpha4/7 and alpha4/4, conotoxins may be important for binding to the alpha3 and/or alpha6, subunit of nAChR.
About this Structure
2I28 is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
NMR structure determination of alpha-conotoxin BuIA, a novel neuronal nicotinic acetylcholine receptor antagonist with an unusual 4/4 disulfide scaffold., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem Biophys Res Commun. 2006 Nov 3;349(4):1228-34. Epub 2006 Sep 7. PMID:16979596
Page seeded by OCA on Wed Nov 21 12:06:47 2007
