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'''COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8''' | '''COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8''' | ||
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[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
[[Category: Grams, F.]] | [[Category: Grams, F.]] | ||
[[Category: | [[Category: Collagen degradation]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Metalloprotease]] | ||
[[Category: | [[Category: Metzincin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:24:54 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 01:24, 3 May 2008
COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8
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 Page seeded by OCA on Sat May 3 01:24:54 2008