2e3x | pdb_00002e3x
Crystal structure of Russell's viper venom metalloproteinase
Structural highlights
FunctionVM3CX_DABSI Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.[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 PubMedRussell's viper venom factor X activator (RVV-X) is a heterotrimeric metalloproteinase with a mammalian ADAM-like heavy chain and two lectin-like light chains. The crystal structure of RVV-X has been determined at 2.9 A resolution and shows a hook-spanner-wrench-like architecture, in which the metalloproteinase/disintegrin region constitutes a hook, and the lectin-like domains constitute a handle. A 6.5nm separation between the catalytic site and a putative exosite suggests a docking model for factor X. The structure provides a typical example of the molecular evolution of multi-subunit proteins and insights into the molecular basis of target recognition and proteolysis by ADAM/adamalysin/reprolysin proteinases. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases.,Takeda S, Igarashi T, Mori H FEBS Lett. 2007 Dec 22;581(30):5859-64. Epub 2007 Dec 3. PMID:18060879[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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