Abstract.
Thrombin is a serine proteinase that can interact with a large number of diverse macromolecular substrates, which results in either a procoagulant or anticoagulant effect. These divergent properties are physiologically regulated by the endogenous protein thrombomodulin. This review summarizes recent work on a variety of methods used to exploit the allosteric nature of the enzyme. The procoagulant and anticoagulant functions of thrombin can be modulated by sodium binding, site-directed mutagenesis, and a small synthetic molecule. Modulation of thrombin's intrinsic properties represents a novel approach to the development of unique antithrombotic agents.
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Hall, S., Gibbs, C. & Leung, L. Strategies for development of novel antithrombotics: modulating thrombin's procoagulant and anticoagulant properties. CMLS, Cell. mol. life sci. 53, 731–736 (1997). https://doi.org/10.1007/s000180050092
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DOI: https://doi.org/10.1007/s000180050092