3s9a: Difference between revisions
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<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=3s9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s9a RCSB], [http://www.ebi.ac.uk/pdbsum/3s9a PDBsum]</span></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=3s9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s9a RCSB], [http://www.ebi.ac.uk/pdbsum/3s9a PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/VSPG_DABSI VSPG_DABSI]] Venom serine protease that selectively activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma.<ref>PMID:3053712</ref> | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 01:09, 25 December 2014
Russell's viper venom serine proteinase, RVV-V (closed-form)Russell's viper venom serine proteinase, RVV-V (closed-form)
Structural highlights
Function[VSPG_DABSI] Venom serine protease that selectively activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma.[1] Publication Abstract from PubMedRussell's viper venom factor V (FV) activator (RVV-V) is a thrombin-like proteinase that specifically cleaves the Arg1545-Ser1546 bond of FV. Here we present the crystal structure of RVV-V in complex with the FV14 peptide (residues 1533-1546 of human FV) determined at 1.8A resolution. The structure reveals multiple interactions between RVV-V and the seven residues, Ile1539 (P(7))-Arg1545 (P(1)), of the cleaved substrate. Comparison with substrate-free structures reveals conformational changes of the RVV-V loops upon substrate binding, suggesting that the multiple interactions are mediated by an induced-fit mechanism. The results provide an explanation for the narrow specificity of RVV-V. Structural basis of coagulation factor V recognition for cleavage by RVV-V.,Nakayama D, Ben Ammar Y, Miyata T, Takeda S FEBS Lett. 2011 Aug 23. PMID:21871889[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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