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.
Perona
J J
JJ
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
Craik
C S
CS
D000595:Amino Acid Sequence; D001665:Binding Sites; D004252:DNA Mutational Analysis; D008969:Molecular Sequence Data; D015202:Protein Engineering; D012697:Serine Endopeptidases / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D012697:Serine Endopeptidases