1kbc: Difference between revisions

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[[Image:1kbc.jpg|left|200px]]
{{Seed}}
[[Image:1kbc.png|left|200px]]


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{{STRUCTURE_1kbc|  PDB=1kbc  |  SCENE=  }}  
{{STRUCTURE_1kbc|  PDB=1kbc  |  SCENE=  }}  


'''PROCARBOXYPEPTIDASE TERNARY COMPLEX'''
===PROCARBOXYPEPTIDASE TERNARY COMPLEX===




==Overview==
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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.
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{{ABSTRACT_PUBMED_9249047}}


==About this Structure==
==About this Structure==
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[[Category: Metalloproteinase]]
[[Category: Metalloproteinase]]
[[Category: Mmp-8]]
[[Category: Mmp-8]]
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Revision as of 07:04, 2 July 2008

File:1kbc.png

Template:STRUCTURE 1kbc

PROCARBOXYPEPTIDASE TERNARY COMPLEX

Template:ABSTRACT PUBMED 9249047

About this Structure

1KBC is a Single protein structure of sequence from Homo sapiens. 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

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