Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction.

Abstract

Expressed in a kinetically trapped folding state, a serpin couples the thermodynamic driving force of a massive beta-sheet rearrangement to the inhibition of a target protease. Hence, the serpin-protease interaction is the premier example of a "spring-loaded" protein-protein interaction. Amino acid substitutions in the hinge region of a serpin reactive loop… (More)

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