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Structural basis of substrate specificity in the serine proteases

Structural basis of substrate specificity in the serine proteases 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Protein Science Wiley

Structural basis of substrate specificity in the serine proteases

Protein Science , Volume 4 (3) – Mar 1, 1995

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References (211)

Publisher
Wiley
Copyright
Copyright © 1995 The Protein Society
ISSN
0961-8368
eISSN
1469-896X
DOI
10.1002/pro.5560040301
pmid
7795518
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Protein ScienceWiley

Published: Mar 1, 1995

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