1wvr: Difference between revisions
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[[Image:1wvr.gif|left|200px]] | [[Image:1wvr.gif|left|200px]] | ||
'''Crystal Structure of a CRISP family Ca-channel blocker derived from snake venom''' | {{Structure | ||
|PDB= 1wvr |SIZE=350|CAPTION= <scene name='initialview01'>1wvr</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of a CRISP family Ca-channel blocker derived from snake venom''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1WVR is a [ | 1WVR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trimeresurus_flavoviridis Trimeresurus flavoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVR OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15953617 15953617] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trimeresurus flavoviridis]] | [[Category: Trimeresurus flavoviridis]] | ||
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[[Category: cysteine-rich secretory protein]] | [[Category: cysteine-rich secretory protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:02:08 2008'' | ||
Revision as of 13:02, 20 March 2008
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| 1wvr, resolution 2.40Å | |||||||||||||
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| Ligands: | CD | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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