1wvr: Difference between revisions

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[[Image:1wvr.gif|left|200px]]
[[Image:1wvr.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wvr OCA], [http://www.ebi.ac.uk/pdbsum/1wvr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wvr RCSB]</span>
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'''Crystal Structure of a CRISP family Ca-channel blocker derived from snake venom'''
'''Crystal Structure of a CRISP family Ca-channel blocker derived from snake venom'''
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[[Category: Suto, K.]]
[[Category: Suto, K.]]
[[Category: Yamazaki, Y.]]
[[Category: Yamazaki, Y.]]
[[Category: cysteine-rich secretory protein]]
[[Category: Cysteine-rich secretory protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:12:10 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:41:38 2008''

Revision as of 11:12, 3 May 2008

File:1wvr.gif

Template:STRUCTURE 1wvr

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. 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 Page seeded by OCA on Sat May 3 14:12:10 2008

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