1mnc

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1mnc, resolution 2.1Å

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STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET

Overview

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 Structure

1MNC is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Interstitial collagenase, with EC number 3.4.24.7 Full crystallographic information is available from OCA.

Reference

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

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