Structure and interaction modes of thrombin.
Any vascular injury triggers the burst-like release of the trypsin-like serine proteinase alpha-thrombin. Thrombin, the main executioner of the coagulation cascade, exhibits procoagulant as well as anticoagulant and antifibrinolytic properties, very specifically interacting with a number of protein substrates, receptors, cofactors, inhibitors, carbohydrates, and modulators. A large number of crystal structures of alpha-thrombin have shown that the thrombin surface can be subdivided into several functional regions, which recognize different substrates, inhibitors, and mediators with high specificity.
Bode
Wolfram
W
Proteinase Research Group, Max-Planck-Institute für Biochemie, Am Klopferspitz 18, D-82152 Martinsried, Germany. bode@biochem.mpg.de
D001665:Binding Sites; D006706:Homeostasis; D006801:Humans; D011485:Protein Binding; D013379:Substrate Specificity; D013917:Thrombin / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology
D013917:Thrombin