1mmb
COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8
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OverviewOverview
Matrix metalloproteinases are a family of zinc endopeptidases involved in, tissue remodeling. They have been implicated in various disease processes, including metastasis, joint destruction, and neurodegeneration. Human, neutrophil collagenase (HNC, MMP-8) represents one of the three, "interstitial" collagenases that cleave triple-helical collagens types I, II, and III. Its 163-residue catalytic domain (Met80 to Gly242) has been, expressed in Escherichia coli and crystallized as a noncovalent complex, with the hydroxamate inhibitor batimastat. The crystal structure, refined, to 2.1 A, demonstrates that batimastat binds to the S1-S2' sites and, coordinates to the catalytic zinc in a bidentate manner via the hydroxyl, and carbonyl oxygens of the hydroxamate group. The batimastat-collagenase, complex is described in detail, and the activities of batimastat analogues, are discussed in the light of the protein-inhibitor interactions revealed, by the crystallography studies.
About this StructureAbout this Structure
1MMB is a Single protein structure of sequence from Homo sapiens with CA, ZN and BAT as ligands. Active as Neutrophil collagenase, with EC number 3.4.24.34 Full crystallographic information is available from OCA.
ReferenceReference
Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor., Grams F, Crimmin M, Hinnes L, Huxley P, Pieper M, Tschesche H, Bode W, Biochemistry. 1995 Oct 31;34(43):14012-20. PMID:7577999
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