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Thrombin Interactions*

Enrico Di Cera, MD
Author and Funding Information

*From the Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO.

Correspondence to: Enrico Di Cera, MD, Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Box 8231, St. Louis, MO 63110; e-mail: enrico@biochem.wustl.edu



Chest. 2003;124(3_suppl):11S-17S. doi:10.1378/chest.124.3_suppl.11S
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After generation from prothrombin, thrombin plays multiple roles in the blood coagulation cascade that are mediated by interaction with a number of physiologic substrates, effectors, and inhibitors. Structural and mutagenesis studies have helped unravel the molecular basis of thrombin interactions in the context of both well-established and emerging new roles of the enzyme. The functional versatility of thrombin owes much to its evolutionary origin and results from structural determinants and mechanisms that can be exploited by pharmacologic intervention.

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thrombin

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