1MMB

COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8

Summary for 1MMB

• Entry DOI: 10.2210/pdb1mmb/pdb
• Descriptor: MATRIX METALLOPROTEINASE-8, CALCIUM ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: hydrolase, metalloprotease, metzincins, collagen degradation, hydrolase (metalloprotease)
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasmic granule: P22894
• Total number of polymer chains: 1
• Total formula weight: 18800.36

Authors

Bode, W.,Grams, F. (deposition date: 1995-08-23, release date: 1996-10-14, Last modification date: 2024-02-14)

Primary citation

Grams, F.,Crimmin, M.,Hinnes, L.,Huxley, P.,Pieper, M.,Tschesche, H.,Bode, W.
Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor.
Biochemistry, 34:14012-14020, 1995

PubMed Abstract: 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.

PubMed: 7577999
DOI: 10.1021/bi00043a007

Experimental method

X-RAY DIFFRACTION (2.1 Å)