1mmb: Difference between revisions

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[[Image:1mmb.gif|left|200px]]
{{Seed}}
[[Image:1mmb.png|left|200px]]


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{{STRUCTURE_1mmb|  PDB=1mmb  |  SCENE=  }}  
{{STRUCTURE_1mmb|  PDB=1mmb  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_7577999}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7577999 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7577999}}


==About this Structure==
==About this Structure==
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[[Category: Metalloprotease]]
[[Category: Metalloprotease]]
[[Category: Metzincin]]
[[Category: Metzincin]]
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