1mmb
From Proteopedia
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- | [[Image:1mmb.gif|left|200px]] | + | [[Image:1mmb.gif|left|200px]] |
- | + | ||
- | '''COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8''' | + | {{Structure |
+ | |PDB= 1mmb |SIZE=350|CAPTION= <scene name='initialview01'>1mmb</scene>, resolution 2.1Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=BAT:4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-METHYLAMIDE'>BAT</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Neutrophil_collagenase Neutrophil collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.34 3.4.24.34] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1MMB is a [ | + | 1MMB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMB OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7577999 7577999] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Neutrophil collagenase]] | [[Category: Neutrophil collagenase]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
- | [[Category: | + | [[Category: metzincin]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:45:16 2008'' |
Revision as of 10:45, 20 March 2008
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, resolution 2.1Å | |||||||
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Ligands: | , and | ||||||
Activity: | Neutrophil collagenase, with EC number 3.4.24.34 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8
Overview
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 Structure
1MMB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Thu Mar 20 12:45:16 2008
Categories: Homo sapiens | Neutrophil collagenase | Single protein | Bode, W. | Grams, F. | BAT | CA | ZN | Collagen degradation | Hydrolase | Metalloprotease | Metzincin