4.0 Article Proceedings Paper

Structure and interaction modes of thrombin

Journal

BLOOD CELLS MOLECULES AND DISEASES
Volume 36, Issue 2, Pages 122-130

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bcmd.2005.12.027

Keywords

thrombin; coagulation; specificity; anion-binding exosite; fibrin; thrombomodulin; cofactors; crystal structures

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Any vascular injury triggers the burst-like release of the trypsin-like serine proteinase a-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 a-thrombin have shown that the thrombin surface can be subdivided into several functional regions, which recognize different substrates, inhibitors, and mediators with high specificity. (c) 2005 Elsevier Inc. All rights reserved.

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