5mhm | pdb_00005mhm

FXIIIa in complex with the inhibitor ZED1630

spinqualitylabelsall models 5mhm, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mhm is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL, GOL, SO4 NonStd Res: 1TX, 7NW, NH2, NLE Related: 4kty Activity: Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [F13A_HUMAN] Defects in F13A1 are the cause of factor XIII subunit A deficiency (FA13AD) [MIM:613225]. FA13AD is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women. Function [F13A_HUMAN] Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. Publication Abstract from PubMed On active duty: The available drugs for cardiovascular diseases can promote blood clotting but can also lead to life-threatening bleeding episodes. A promising target for the development of safer alternatives is the transglutaminase Factor XIII (FXIII), the active structure of which is presented. The binding and coordination of three calcium ions induce major domain movements in the enzyme upon activation. Structure of Active Coagulation Factor XIII Triggered by Calcium Binding: Basis for the Design of Next-Generation Anticoagulants.,Stieler M, Weber J, Hils M, Kolb P, Heine A, Buchold C, Pasternack R, Klebe G Angew Chem Int Ed Engl. 2013 Sep 20. doi: 10.1002/anie.201305133. PMID:24115223 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Factor XIII

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