4gso
structure of Jararacussin-I
Structural highlights
FunctionVSP1_BOTJR Thrombin-like enzyme that shows clotting activity upon human plasma. Shows specific fibrinogenolytic activity for Aalpha chain (FGA). Hydrolyzes fibrin, BAPNA and TAME, as well as chromogenic artificial substrates of the blood coagulation cascasde: S-27654 for factor X (F10), S-2302 for kallikrein (KLK), factor XIa (F11), and XIIa (F12), and S-2266 for kallikrein and factor XIa (F11). Subcutaneous injection into mice induces a mild edema. Intravenous and intramuscular injection reduce plasma fibrinogen concentration and increase the levels of fibrin(ogen) degradation products. Intramuscular injection also promotes an increase in the expression of proMMP-9, but is unable to activate it.[1] [2] [3] Publication Abstract from PubMedSnake venom serine proteinases (SVSPs) are hemostatically-active toxins that perturb the maintenance and regulation of both the blood coagulation cascade and fibrinolytic feedback system at specific points, and hence, are widely used as tools in pharmacological and clinical diagnosis. The crystal structure of a thrombin-like enzyme (TLE) from Bothrops jararacussu venom (Jararacussin-I) was determined at 2.48 A resolution. This is the first crystal structure of a TLE and permits structural comparisons with both the Agkistrodon contortrix contortrix Protein C Activator (ACC-C) and the Trimeresurus stejnegeri plasminogen activator (TSV-PA). Despite the highly conserved overall fold, significant differences in the amino acid compositions and three-dimensional conformations of the loops surrounding the active site significantly alter the molecular topography and charge distribution profile of the catalytic interface. In contrast to other SVSPs, the catalytic interface of Jararacussin-I is highly negatively charged, which contributes to its unique macromolecular selectivity. Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes.,Ullah A, Souza TC, Zanphorlin LM, Mariutti RB, Santana VS, Murakami MT, Arni RK Protein Sci. 2012 Nov 8. doi: 10.1002/pro.2189. PMID:23139169[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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