Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization

<table>The scheme shown here (taking antithrombin as an example) represents the suicide substrate inhibition mechanism common to all inhibitory serpins.  The scheme represents the interaction between the serpin (antithrombin, ATIII) and protease (E); ATIII-E is the noncovalent Michaelis complex; ATIII-E’ is the proposed intermediate before partitioning; ATIII-E* is the stable protease-inhibitor complex; ATIII* is the cleaved ATIII.  The outcome of the reaction is dependent on the partitioning between the inhibitory (<i>k </i><sub>inh</sub>) and substrate pathways (<i>k </i><sub>sub</sub>). The figures represent the cleaved and factor Xa bound ternary complexes of antithrombin [<a href="../#B3">3</a>].</table>

Journal of Amino Acids

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Figure 1

Figure 1: Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization 