1dx5
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CRYSTAL STRUCTURE OF THE THROMBIN-THROMBOMODULIN COMPLEX
OverviewOverview
The serine proteinase alpha-thrombin causes blood clotting through, proteolytic cleavage of fibrinogen and protease-activated receptors and, amplifies its own generation by activating the essential clotting factors, V and VIII. Thrombomodulin, a transmembrane thrombin receptor with six, contiguous epidermal growth factor-like domains (TME1-6), profoundly, alters the substrate specificity of thrombin from pro- to anticoagulant by, activating protein C. Activated protein C then deactivates the coagulation, cascade by degrading activated factors V and VIII. The, thrombin-thrombomodulin complex inhibits fibrinolysis by activating the, procarboxypeptidase thrombin-activatable fibrinolysis inhibitor. Here we, present the 2.3 A crystal structure of human alpha-thrombin bound to the, smallest ... [(full description)]
About this StructureAbout this Structure
1DX5 is a [Protein complex] structure of sequences from [Homo sapiens] with NDG, CA, NA and FMT as [ligands]. Active as [Thrombin], with EC number [3.4.21.5]. Structure known Active Sites: AC1, AC2, AC3 and AC4. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex., Fuentes-Prior P, Iwanaga Y, Huber R, Pagila R, Rumennik G, Seto M, Morser J, Light DR, Bode W, Nature. 2000 Mar 30;404(6777):518-25. PMID:10761923
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