1MNC

STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET

Summary for 1MNC

• Entry DOI: 10.2210/pdb1mnc/pdb
• Descriptor: NEUTROPHIL COLLAGENASE, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase (metalloprotease)
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 18399.78

Authors

Stams, T.,Spurlino, J.C.,Smith, D.L.,Rubin, B. (deposition date: 1994-01-12, release date: 1995-02-07, Last modification date: 2024-02-14)

Primary citation

Stams, T.,Spurlino, J.C.,Smith, D.L.,Wahl, R.C.,Ho, T.F.,Qoronfleh, M.W.,Banks, T.M.,Rubin, B.
Structure of human neutrophil collagenase reveals large S1' specificity pocket.
Nat.Struct.Biol., 1:119-123, 1994

PubMed Abstract: 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.

PubMed: 7656015
DOI: 10.1038/nsb0294-119

Experimental method

X-RAY DIFFRACTION (2.1 Å)