View source for 3sbk


==Russell's viper venom serine proteinase, RVV-V (PPACK-bound form)==
<StructureSection load='3sbk' size='340' side='right'caption='[[3sbk]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sbk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_siamensis Daboia siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SBK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0G6:D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PROLINAMIDE'>0G6</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3sbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbk OCA], [https://pdbe.org/3sbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sbk RCSB], [https://www.ebi.ac.uk/pdbsum/3sbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbk ProSAT]</span></td></tr>
</table>
== Function ==
[https://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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Russell'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<ref>PMID:21871889</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3sbk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Daboia siamensis]]
[[Category: Large Structures]]
[[Category: Ben Ammar Y]]
[[Category: Nakayama D]]
[[Category: Takeda S]]