1wvr
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(New page: 200px<br /><applet load="1wvr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wvr, resolution 2.40Å" /> '''Crystal Structure of...)
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Revision as of 03:35, 21 November 2007
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Crystal Structure of a CRISP family Ca-channel blocker derived from snake venom
Overview
The cysteine-rich secretory proteins (CRISPs) are widely distributed in, mammals, reptiles, amphibians and secernenteas, and are involved in a, variety of biological reactions. Here we report the crystal structure of, triflin, a snake venom derived blocker of high K(+)-induced artery, contraction, at 2.4A resolution. Triflin consists of two domains. The, first 163 residues form a large globular body with an alpha-beta-alpha, sandwich core, which resembles pathogenesis-related proteins of group-1, (PR-1). Two glutamic acid-associated histidine residues are located in an, elongated cleft. A Cd(2+) resides in this binding site, and forms a, five-coordination sphere. The subsequent cysteine-rich domain adopts a, rod-like shape, which is stabilized by five disulfide bridges. Hydrophobic, residues, which may obstruct the target ion-channel, are exposed to the, solvent. A concave surface, which is surrounded by these two domains, is, also expected to play a significant role in the binding to the target, receptor, leading to ion channel blockage. The C-terminal cysteine-rich, region has a similar tertiary structure to voltage-gated potassium channel, blocker toxins, such as BgK and ShK. These findings will contribute toward, understanding the functions of the widely distributed CRISP family, proteins.
About this Structure
1WVR is a Single protein structure of sequence from Trimeresurus flavoviridis with CD as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a CRISP family Ca2+ -channel blocker derived from snake venom., Shikamoto Y, Suto K, Yamazaki Y, Morita T, Mizuno H, J Mol Biol. 2005 Jul 22;350(4):735-43. PMID:15953617
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