1dg2
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(New page: 200px<br /><applet load="1dg2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dg2" /> '''SOLUTION CONFORMATION OF A-CONOTOXIN AUIB'''...)
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Revision as of 11:08, 20 November 2007
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SOLUTION CONFORMATION OF A-CONOTOXIN AUIB
Overview
The neuronal nicotinic acetylcholine receptors constitute a highly diverse, group, with subtypes consisting of pentameric combinations of alpha and, beta subunits. alpha-Conotoxins are a homologous series of small peptides, that antagonize these receptors. We present the three-dimensional solution, structure of alpha-conotoxin AuIB, the first 15-residue alpha-conotoxin, known to selectively block the alpha(3)beta(4) nicotinic acetylcholine, receptor subtype. The pairwise backbone and heavy-atom root mean square, deviation for an ensemble of 20 structures are 0.269 and 0.720 A, respectively. The overall fold of alpha-conotoxin AuIB closely resembles, that of the alpha4/7 subfamily alpha-conotoxins. However, the absence of, Tyr(15), normally present in other alpha4/7 members, results in tight, bending of the backbone at the C terminus and effectively renders Asp(14), to assume the spatial location of Tyr(15) present in other neuronal, alpha4/7 alpha-conotoxins. Structural comparison of alpha-conotoxin AuIB, with the alpha(3)beta(2) subtype-specific alpha-conotoxin MII shows, different electrostatic surface charge distributions, which may be, important in differential receptor subtype recognition.
About this Structure
1DG2 is a Single protein structure of sequence from Conus aulicus with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Nuclear magnetic resonance solution conformation of alpha-conotoxin AuIB, an alpha(3)beta(4) subtype-selective neuronal nicotinic acetylcholine receptor antagonist., Cho JH, Mok KH, Olivera BM, McIntosh JM, Park KH, Han KH, J Biol Chem. 2000 Mar 24;275(12):8680-5. PMID:10722709
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