1mnc
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STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET
OverviewOverview
The crystal structure of the catalytic domain of human neutrophil, collagenase complexed with a peptide transition state analogue has been, determined to a resolution of 2.1 A. The structure of the neutrophil, enzyme, when compared with the three dimensional structure of the, corresponding human fibroblast collagenase, shows differences in the, first, S1', of the three enzyme specificity subsites on the, carboxy-terminal side of the substrate scissile bond. The S1' pocket in, the neutrophil collagenase is significantly larger than the equivalent, site in the fibroblast enzyme, suggesting that the former enzyme has a, broader range of possible substrates. Such differences also suggest, approaches for the design of selective matrix metalloproteinase, inhibitors.
About this StructureAbout this Structure
1MNC is a Single protein structure of sequence from Homo sapiens with ZN, CA and PLH as ligands. Active as Interstitial collagenase, with EC number 3.4.24.7 Full crystallographic information is available from OCA.
ReferenceReference
Structure of human neutrophil collagenase reveals large S1' specificity pocket., Stams T, Spurlino JC, Smith DL, Wahl RC, Ho TF, Qoronfleh MW, Banks TM, Rubin B, Nat Struct Biol. 1994 Feb;1(2):119-23. PMID:7656015
Page seeded by OCA on Mon Nov 12 18:13:19 2007