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Structure and interaction modes of thrombin

Wolfram Bode1

  • 1Proteinase Research Group, Max-Planck-Institute für Biochemie, Am Klopferspitz 18, D-82152 Martinsried, Germany. bode@biochem.mpg.de

Blood Cells, Molecules & Diseases
|February 17, 2006
PubMed

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.

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