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1wvr

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Crystal Structure of a CRISP family Ca-channel blocker derived from snake venom

Structural highlights

1wvr is a 1 chain structure with sequence from Protobothrops flavoviridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CRVP_PROFL Blocks contraction of smooth muscle elicited by high potassium-induced depolarization (PubMed:12047379). May target voltage-gated calcium channels (Cav) on smooth muscle.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yamazaki Y, Koike H, Sugiyama Y, Motoyoshi K, Wada T, Hishinuma S, Mita M, Morita T. Cloning and characterization of novel snake venom proteins that block smooth muscle contraction. Eur J Biochem. 2002 Jun;269(11):2708-15. PMID:12047379
↑ Shikamoto Y, Suto K, Yamazaki Y, Morita T, Mizuno H. Crystal structure of a CRISP family Ca2+ -channel blocker derived from snake venom. J Mol Biol. 2005 Jul 22;350(4):735-43. PMID:15953617 doi:10.1016/j.jmb.2005.05.020

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wvr"

@@ Line 3: / Line 3: @@
 <StructureSection load='1wvr' size='340' side='right'caption='[[1wvr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wvr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bothrops_flavoviridis Bothrops flavoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WVR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wvr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Protobothrops_flavoviridis Protobothrops flavoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WVR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wvr OCA], [https://pdbe.org/1wvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wvr RCSB], [https://www.ebi.ac.uk/pdbsum/1wvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wvr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CRVP_PROFL CRVP_PROFL]] Blocks contraction of smooth muscle elicited by high potassium-induced depolarization (PubMed:12047379). May target voltage-gated calcium channels (Cav) on smooth muscle.<ref>PMID:12047379</ref>
+[https://www.uniprot.org/uniprot/CRVP_PROFL CRVP_PROFL] Blocks contraction of smooth muscle elicited by high potassium-induced depolarization (PubMed:12047379). May target voltage-gated calcium channels (Cav) on smooth muscle.<ref>PMID:12047379</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bothrops flavoviridis]]
 [[Category: Large Structures]]
-[[Category: Mizuno, H]]
+[[Category: Protobothrops flavoviridis]]
-[[Category: Morita, T]]
+[[Category: Mizuno H]]
-[[Category: Shikamoto, Y]]
+[[Category: Morita T]]
-[[Category: Suto, K]]
+[[Category: Shikamoto Y]]
-[[Category: Yamazaki, Y]]
+[[Category: Suto K]]
-[[Category: Cysteine-rich secretory protein]]
+[[Category: Yamazaki Y]]
-[[Category: Toxin]]

1wvr

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Current revision

Crystal Structure of a CRISP family Ca-channel blocker derived from snake venom

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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