2tcl
From Proteopedia
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|PDB= 2tcl |SIZE=350|CAPTION= <scene name='initialview01'>2tcl</scene>, resolution 2.20Å | |PDB= 2tcl |SIZE=350|CAPTION= <scene name='initialview01'>2tcl</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=RO4:[[1-[N-HYDROXY-ACETAMIDYL]-3-METHYL-BUTYL]-CARBONYL-LEUCINYL]-ALANINE+ETHYL+ESTER'>RO4</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2tcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tcl OCA], [http://www.ebi.ac.uk/pdbsum/2tcl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2tcl RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
In rheumatoid and osteoarthritis, degradation of articular cartilage is mediated by the matrix metalloproteinases collagenase, stromelysin and gelatinase. The key event in this process is the cleavage of triple helical collagen by collagenase. We have determined the crystal structure of the catalytic domain of human recombinant fibroblast collagenase complexed with a synthetic inhibitor at 2.2 A resolution. The protein fold is similar to the amino termini of the zinc endopeptidases astacin thermolysin and elastase despite a lack of primary sequence homology. The conformation of the bound inhibitor provides a molecular basis for the design of inhibitors of collagenase and other matrix metalloproteinases. Such inhibitors should be useful in the treatment of a variety of diseases including arthritis and cancer. | In rheumatoid and osteoarthritis, degradation of articular cartilage is mediated by the matrix metalloproteinases collagenase, stromelysin and gelatinase. The key event in this process is the cleavage of triple helical collagen by collagenase. We have determined the crystal structure of the catalytic domain of human recombinant fibroblast collagenase complexed with a synthetic inhibitor at 2.2 A resolution. The protein fold is similar to the amino termini of the zinc endopeptidases astacin thermolysin and elastase despite a lack of primary sequence homology. The conformation of the bound inhibitor provides a molecular basis for the design of inhibitors of collagenase and other matrix metalloproteinases. Such inhibitors should be useful in the treatment of a variety of diseases including arthritis and cancer. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120353 120353]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Borkakoti, N.]] | [[Category: Borkakoti, N.]] | ||
[[Category: Winkler, F K.]] | [[Category: Winkler, F K.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: RO4]] | ||
| - | [[Category: SM]] | ||
| - | [[Category: ZN]] | ||
[[Category: hydrolase (metalloprotease)]] | [[Category: hydrolase (metalloprotease)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:03:33 2008'' |
Revision as of 02:03, 31 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR
Overview
In rheumatoid and osteoarthritis, degradation of articular cartilage is mediated by the matrix metalloproteinases collagenase, stromelysin and gelatinase. The key event in this process is the cleavage of triple helical collagen by collagenase. We have determined the crystal structure of the catalytic domain of human recombinant fibroblast collagenase complexed with a synthetic inhibitor at 2.2 A resolution. The protein fold is similar to the amino termini of the zinc endopeptidases astacin thermolysin and elastase despite a lack of primary sequence homology. The conformation of the bound inhibitor provides a molecular basis for the design of inhibitors of collagenase and other matrix metalloproteinases. Such inhibitors should be useful in the treatment of a variety of diseases including arthritis and cancer.
About this Structure
2TCL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor., Borkakoti N, Winkler FK, Williams DH, D'Arcy A, Broadhurst MJ, Brown PA, Johnson WH, Murray EJ, Nat Struct Biol. 1994 Feb;1(2):106-10. PMID:7656013
Page seeded by OCA on Mon Mar 31 05:03:33 2008
