1mmr
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MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR
OverviewOverview
Matrix metalloproteases are a family of enzymes that play critical roles, in the physiological and pathological degradation of the extracellular, matrix. These enzymes may be important therapeutic targets for the, treatment of various diseases where tissue degradation is part of the, pathology, such as cancer and arthritis. Matrilysin is the smallest member, of this family of enzymes, all of which require zinc for catalytic, activity. The first X-ray crystal structures of human matrilysin are, presented. Inhibitors of metalloproteases are often characterized by the, chemical group that interacts with the active site zinc of the protein., The structures of matrilysin complexed with hydroxamate (maximum, resolution 1.9 A), carboxylate (maximum resolution 2.4 A), and, sulfodiimine (maximum resolution 2.3 A) inhibitors are presented here and, provide detailed information about how each functional group interacts, with the catalytic zinc. Only the zinc-coordination group is variable in, this series of inhibitors. Examination of these inhibitor-matrilysin, complexes emphasizes the dominant role the zinc-coordinating group plays, in determining the relative potencies of the inhibitors. The structures of, these matrilysin-inhibitor complexes also provide a basis for comparing, the catalytic mechanism of MMPs and other metalloproteins.
About this StructureAbout this Structure
1MMR is a Single protein structure of sequence from Homo sapiens with ZN, CA and SRS as ligands. Active as Matrilysin, with EC number 3.4.24.23 Full crystallographic information is available from OCA.
ReferenceReference
Matrilysin-inhibitor complexes: common themes among metalloproteases., Browner MF, Smith WW, Castelhano AL, Biochemistry. 1995 May 23;34(20):6602-10. PMID:7756291
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