1kbc
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Matrix metalloproteinases (MMP) are zinc endopeptidases involved in tissue | + | Matrix metalloproteinases (MMP) are zinc endopeptidases involved in tissue remodelling. They have been implicated in a series of pathologies, including cancer, arthritis, joint destruction and Alzheimer's disease. Human neutrophil collagenase represents one of the three interstitial collagenases that cleave triple-helical collagen of type I, II and III. Its catalytic domain (residues Phe79-Gly242) has been heterologously expressed in Escherichia coli and crystallized as a non-covalent complex with the hydroxamate inhibitor BB-1909, which has distinct selectivity against different MMP, in a crystal form. The crystal structure, refined to 0.18-nm resolution, shows that BB-1909 is a right-hand-side inhibitor that binds to the S1'-S3' subsites and coordinates to the catalytic Zn2+ in a bidentate manner via the hydroxyl and carbonyl oxygen atoms of the hydroxamate group in a similar manner to batimastat. The collagenase/BB-1909 complex is described in detail and compared with the collagenase/batimastat complex. These studies provide information on MMP specificity and thus may assist the development of more-selective MMP inhibitors. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Betz, M.]] | [[Category: Betz, M.]] | ||
[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
| - | [[Category: Gomis-Rueth, F | + | [[Category: Gomis-Rueth, F X.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: HLE]] | [[Category: HLE]] | ||
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[[Category: mmp-8]] | [[Category: mmp-8]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:10 2008'' |
Revision as of 11:32, 21 February 2008
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PROCARBOXYPEPTIDASE TERNARY COMPLEX
Overview
Matrix metalloproteinases (MMP) are zinc endopeptidases involved in tissue remodelling. They have been implicated in a series of pathologies, including cancer, arthritis, joint destruction and Alzheimer's disease. Human neutrophil collagenase represents one of the three interstitial collagenases that cleave triple-helical collagen of type I, II and III. Its catalytic domain (residues Phe79-Gly242) has been heterologously expressed in Escherichia coli and crystallized as a non-covalent complex with the hydroxamate inhibitor BB-1909, which has distinct selectivity against different MMP, in a crystal form. The crystal structure, refined to 0.18-nm resolution, shows that BB-1909 is a right-hand-side inhibitor that binds to the S1'-S3' subsites and coordinates to the catalytic Zn2+ in a bidentate manner via the hydroxyl and carbonyl oxygen atoms of the hydroxamate group in a similar manner to batimastat. The collagenase/BB-1909 complex is described in detail and compared with the collagenase/batimastat complex. These studies provide information on MMP specificity and thus may assist the development of more-selective MMP inhibitors.
About this Structure
1KBC is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Neutrophil collagenase, with EC number 3.4.24.34 Full crystallographic information is available from OCA.
Reference
1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile., Betz M, Huxley P, Davies SJ, Mushtaq Y, Pieper M, Tschesche H, Bode W, Gomis-Ruth FX, Eur J Biochem. 1997 Jul 1;247(1):356-63. PMID:9249047
Page seeded by OCA on Thu Feb 21 13:32:10 2008
Categories: Homo sapiens | Neutrophil collagenase | Single protein | Betz, M. | Bode, W. | Gomis-Rueth, F X. | CA | HLE | ZN | Collagenase | Hnc | Hydrolase | Hydrolytic enzyme | Inhibitor | Matrixin | Metalloproteinase | Mmp-8
