1wvr
From Proteopedia
(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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| - | [[Image:1wvr.gif|left|200px]]<br /><applet load="1wvr" size=" | + | [[Image:1wvr.gif|left|200px]]<br /><applet load="1wvr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wvr, resolution 2.40Å" /> | caption="1wvr, resolution 2.40Å" /> | ||
'''Crystal Structure of a CRISP family Ca-channel blocker derived from snake venom'''<br /> | '''Crystal Structure of a CRISP family Ca-channel blocker derived from snake venom'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The cysteine-rich secretory proteins (CRISPs) are widely distributed in | + | 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== | ==About this Structure== | ||
| - | 1WVR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trimeresurus_flavoviridis Trimeresurus flavoviridis] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1WVR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trimeresurus_flavoviridis Trimeresurus flavoviridis] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: cysteine-rich secretory protein]] | [[Category: cysteine-rich secretory protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:34 2008'' |
Revision as of 13:48, 21 February 2008
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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 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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