1kbc: Difference between revisions
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|PDB= 1kbc |SIZE=350|CAPTION= <scene name='initialview01'>1kbc</scene>, resolution 1.8Å | |PDB= 1kbc |SIZE=350|CAPTION= <scene name='initialview01'>1kbc</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HLE:3-FORMYL-2-HYDROXY-5-METHYL-HEXANOIC+ACID+HYDROXYAMIDE'>HLE</scene>, <scene name='pdbligand=RIN:3-AMINO-AZACYCLOTRIDECAN-2-ONE'>RIN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kbc OCA], [http://www.ebi.ac.uk/pdbsum/1kbc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kbc RCSB]</span> | |||
}} | }} | ||
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[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
[[Category: Gomis-Rueth, F X.]] | [[Category: Gomis-Rueth, F X.]] | ||
[[Category: collagenase]] | [[Category: collagenase]] | ||
[[Category: hnc]] | [[Category: hnc]] | ||
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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 Sun Mar 30 21:46:05 2008'' | ||
Revision as of 21:46, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Neutrophil collagenase, with EC number 3.4.24.34 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PROCARBOXYPEPTIDASE TERNARY COMPLEX
OverviewOverview
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 StructureAbout this Structure
1KBC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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