3s9c
From Proteopedia
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| - | [[Image:3s9c.jpg|left|200px]]  | ||
| - | + | ==Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V==  | |
| - | + | <StructureSection load='3s9c' size='340' side='right'caption='[[3s9c]], [[Resolution|resolution]] 1.80Å' scene=''>  | |
| - | + | == Structural highlights ==  | |
| - | + | <table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_siamensis Daboia siamensis] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S9C 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]] 1.8Å</td></tr>  | |
| - | -  | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3s9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9c OCA], [https://pdbe.org/3s9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s9c RCSB], [https://www.ebi.ac.uk/pdbsum/3s9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s9c 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>  | ||
| + | </div>  | ||
| + | <div class="pdbe-citations 3s9c" style="background-color:#fffaf0;"></div>  | ||
| - | + | ==See Also==  | |
| - | + | *[[Proteinase 3D structures|Proteinase 3D structures]]  | |
| - | + | == References ==  | |
| - | + | <references/>  | |
| - | + | __TOC__  | |
| - | + | </StructureSection>  | |
| - | ==  | + | [[Category: Daboia siamensis]]  | 
| - | [[  | + | [[Category: Homo sapiens]]  | 
| - | + | [[Category: Large Structures]]  | |
| - | ==  | + | [[Category: Ben Ammar Y]]  | 
| - | <  | + | [[Category: Nakayama D]]  | 
| - | [[Category: Daboia   | + | [[Category: Takeda S]]  | 
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Current revision
Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V
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