Structural highlights
2e3x is a 3 chain structure with sequence from Daboia russellii siamensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| Activity: | Russellysin, with EC number 3.4.24.58 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[VM3CX_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] [SLLC1_DABSI] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The 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. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.[2] [SLLC2_DABSI] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The 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. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.[3]
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
Russell'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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen HS, Chen JM, Lin CW, Khoo KH, Tsai IH. New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom. FEBS J. 2008 Aug;275(15):3944-58. Epub 2008 Jul 4. PMID:18616470 doi:http://dx.doi.org/EJB6540
- ↑ Chen HS, Chen JM, Lin CW, Khoo KH, Tsai IH. New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom. FEBS J. 2008 Aug;275(15):3944-58. Epub 2008 Jul 4. PMID:18616470 doi:http://dx.doi.org/EJB6540
- ↑ Chen HS, Chen JM, Lin CW, Khoo KH, Tsai IH. New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom. FEBS J. 2008 Aug;275(15):3944-58. Epub 2008 Jul 4. PMID:18616470 doi:http://dx.doi.org/EJB6540
- ↑ Takeda S, Igarashi T, Mori H. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases. FEBS Lett. 2007 Dec 22;581(30):5859-64. Epub 2007 Dec 3. PMID:18060879 doi:10.1016/j.febslet.2007.11.062
