1. A model of the protein C activation complex
A model of the protein C activation complex. Thrombin binding to thrombomodulin involves anion binding exosite 1 on thrombin (shown as a strip through the middle of thrombin) and EGF domain 4 to 6 on TM. A chondroitin-sulfate moiety on TM increases the affinity for thrombin, but is not required for function. This chondroitin sulfate interacts with anion-binding exosite 2 on thrombin, a second, very basic area near the heparin-binding site. The protein C cleavage site and the thrombin active site are approximately 65 Å from the membrane surface, indicating that TM “lifts” the thrombin off the membrane surface and basically accomplishes the same special functions as those accomplished by the Gla and EGF domains in protein C.
Source: Anticoagulant Protein C/Thrombomodulin Pathway, The Online Metabolic and Molecular Bases of Inherited Disease
Citation: Valle D, Beaudet AL, Vogelstein B, Kinzler KW, Antonarakis SE, Ballabio A, Gibson K, Mitchell G. The Online Metabolic and Molecular Bases of Inherited Disease; 2014 Available at: Accessed: December 27, 2017
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