Title of article :
Structure and interaction modes of thrombin
Author/Authors :
Wolfram Bode، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2006
Abstract :
Any vascular injury triggers the burst-like release of the trypsin-like serine proteinase α-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 α-thrombin have shown that the thrombin surface can be subdivided into several functional regions, which recognize different substrates, inhibitors, and mediators with high specificity.
Keywords :
Anion-binding exosite , Fibrin , thrombomodulin , Cofactors , crystal structures , thrombin , coagulation , specificity
Journal title :
Blood Cells, Molecules and Diseases
Journal title :
Blood Cells, Molecules and Diseases