This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1wvr

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 09:04, 21 April 2021

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

Structural highlights

1wvr is a 1 chain structure with sequence from Bothrops flavoviridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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 [http://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 [http://oca.weizmann.ac.il/oca-docs/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/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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
+</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'>[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://pdbe.org/1wvr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wvr RCSB], [http://www.ebi.ac.uk/pdbsum/1wvr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wvr ProSAT]</span></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 ==
-[[http://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]]

1wvr

From Proteopedia

Revision as of 09:04, 21 April 2021

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

Personal tools

Navigation

Search

Toolbox