1su3: Difference between revisions
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'''X-ray structure of human proMMP-1: New insights into collagenase action''' | {{Structure | ||
|PDB= 1su3 |SIZE=350|CAPTION= <scene name='initialview01'>1su3</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] | |||
|GENE= MMP1, CLG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''X-ray structure of human proMMP-1: New insights into collagenase action''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SU3 is a [ | 1SU3 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=1SU3 OCA]. | ||
==Reference== | ==Reference== | ||
X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding., Jozic D, Bourenkov G, Lim NH, Visse R, Nagase H, Bode W, Maskos K, J Biol Chem. 2005 Mar 11;280(10):9578-85. Epub 2004 Dec 15. PMID:[http:// | X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding., Jozic D, Bourenkov G, Lim NH, Visse R, Nagase H, Bode W, Maskos K, J Biol Chem. 2005 Mar 11;280(10):9578-85. Epub 2004 Dec 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15611040 15611040] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Interstitial collagenase]] | [[Category: Interstitial collagenase]] | ||
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[[Category: prodomain]] | [[Category: prodomain]] | ||
[[Category: spine]] | [[Category: spine]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
''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 14:09:37 2008'' | ||
Revision as of 15:09, 20 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , and | ||||||
| Gene: | MMP1, CLG (Homo sapiens) | ||||||
| Activity: | Interstitial collagenase, with EC number 3.4.24.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray structure of human proMMP-1: New insights into collagenase action
OverviewOverview
Vertebrate collagenases, members of the matrix metalloproteinase (MMP) family, initiate interstitial fibrillar collagen breakdown. It is essential in many biological processes, and unbalanced collagenolysis is associated with diseases such as arthritis, cancer, atherosclerosis, aneurysm, and fibrosis. These metalloproteinases are secreted from the cell as inactive precursors, procollagenases (proMMPs). To gain insights into the structural basis of their activation mechanisms and collagen binding, we have crystallized recombinant human proMMP-1 and determined its structure to 2.2 A resolution. The catalytic metalloproteinase domain and the C-terminal hemopexin (Hpx) domain show the classical MMP-fold, but the structure has revealed new features in surface loops and domain interaction. The prodomain is formed by a three-helix bundle and gives insight into the stepwise activation mechanism of proMMP-1. The prodomain interacts with the Hpx domain, which affects the position of the Hpx domain relative to the catalytic domain. This interaction results in a "closed" configuration of proMMP-1 in contrast to the "open" configuration observed previously for the structure of active MMP-1. This is the first evidence of mobility of the Hpx domain in relation to the catalytic domain, providing an important clue toward the understanding of the collagenase-collagen interaction and subsequent collagenolysis.
DiseaseDisease
Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[120353]
About this StructureAbout this Structure
1SU3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding., Jozic D, Bourenkov G, Lim NH, Visse R, Nagase H, Bode W, Maskos K, J Biol Chem. 2005 Mar 11;280(10):9578-85. Epub 2004 Dec 15. PMID:15611040
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