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Structural basis of substrate specificity in the serine proteases
Author(s) -
Perona John J.,
Craik Charles S.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040301
Subject(s) - proteases , serine protease , substrate specificity , serine , computational biology , function (biology) , flexibility (engineering) , chemistry , protease , biochemistry , biology , genetics , enzyme , mathematics , statistics
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.