Structure and interaction modes of thrombin.

Wolfram Bode

doi:10.1016/j.bcmd.2005.12.027

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Structure and interaction modes of thrombin.

Wolfram Bode

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Abstract

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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Binding Sites Homeostasis Humans Protein Binding Substrate Specificity Thrombin Journal Article Research Support, Non-U.S. Gov't Review

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Wolfram Bode. 2006-02-15. Structure and interaction modes of thrombin.. https://doi.org/10.1016/j.bcmd.2005.12.027

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