1mmb
COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8
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| , resolution 2.1Å | |||||||
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| Ligands: | , and | ||||||
| Activity: | Neutrophil collagenase, with EC number 3.4.24.34 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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