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Protein Science, Vol 4, Issue 3 337-360, Copyright © 1995 by Cold Spring Harbor Laboratory Press

REVIEWS

Structural basis of substrate specificity in the serine proteases

J. J. PERONA and C. S. CRAIK
Present address: Department of Chemistry and Interdepartmental Program in Biochemistry and Molecular Biology, University of California, Santa Barbara, California 93106.

Structure-based mutational analysis of serine protease specificity has produced a large database of information useful in addressing biological function and in establishing a basis for targeted design efforts. Critical issues examined include the function of water molecules in providing strength and specificity of binding, the extent to which binding subsites are interdependent, and the roles of polypeptide chain flexibility and distal structural elements in contributing to specificity profiles. The studies also provide a foundation for exploring why specificity modification can be either straightforward or complex, depending on the particular system.
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