2clt
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The extracellular matrix is a dynamic environment that constantly, undergoes remodelling and degradation during vital physiological processes, such as angiogenesis, wound healing, and development. Unbalanced, extracellular matrix breakdown is associated with many diseases such as, arthritis, cancer and fibrosis. Interstitial collagen is degraded by, matrix metalloproteinases with collagenolytic activity by MMP-1, MMP-8 and, MMP-13, collectively known as the collagenases. Matrix metalloproteinase 1, (MMP-1) plays a pivotal role in degradation of interstitial collagen types, I, II, and III. Here, we report the crystal structure of the active form, of human MMP-1 at 2.67 A resolution. This is the first MMP-1 structure, that is free of inhibitor and a water molecule essential for peptide, .. | + | The extracellular matrix is a dynamic environment that constantly, undergoes remodelling and degradation during vital physiological processes, such as angiogenesis, wound healing, and development. Unbalanced, extracellular matrix breakdown is associated with many diseases such as, arthritis, cancer and fibrosis. Interstitial collagen is degraded by, matrix metalloproteinases with collagenolytic activity by MMP-1, MMP-8 and, MMP-13, collectively known as the collagenases. Matrix metalloproteinase 1, (MMP-1) plays a pivotal role in degradation of interstitial collagen types, I, II, and III. Here, we report the crystal structure of the active form, of human MMP-1 at 2.67 A resolution. This is the first MMP-1 structure, that is free of inhibitor and a water molecule essential for peptide, hydrolysis is observed coordinated with the active site zinc. Comparing, this structure with the human proMMP-1 shows significant structural, differences, mainly in the relative orientation of the hemopexin domain, between the pro form and active form of the human enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 2CLT is a | + | 2CLT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CLT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:52:20 2007'' |
Revision as of 11:47, 5 November 2007
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CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE.
Overview
The extracellular matrix is a dynamic environment that constantly, undergoes remodelling and degradation during vital physiological processes, such as angiogenesis, wound healing, and development. Unbalanced, extracellular matrix breakdown is associated with many diseases such as, arthritis, cancer and fibrosis. Interstitial collagen is degraded by, matrix metalloproteinases with collagenolytic activity by MMP-1, MMP-8 and, MMP-13, collectively known as the collagenases. Matrix metalloproteinase 1, (MMP-1) plays a pivotal role in degradation of interstitial collagen types, I, II, and III. Here, we report the crystal structure of the active form, of human MMP-1 at 2.67 A resolution. This is the first MMP-1 structure, that is free of inhibitor and a water molecule essential for peptide, hydrolysis is observed coordinated with the active site zinc. Comparing, this structure with the human proMMP-1 shows significant structural, differences, mainly in the relative orientation of the hemopexin domain, between the pro form and active form of the human enzyme.
About this Structure
2CLT is a Single protein structure of sequence from Homo sapiens with CA and ZN as ligands. Active as Interstitial collagenase, with EC number 3.4.24.7 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Crystal structure of an active form of human MMP-1., Iyer S, Visse R, Nagase H, Acharya KR, J Mol Biol. 2006 Sep 8;362(1):78-88. Epub 2006 Aug 4. PMID:16890240
Page seeded by OCA on Mon Nov 5 13:52:20 2007
Categories: Homo sapiens | Interstitial collagenase | Single protein | Acharya, K.R. | Iyer, S. | Nagase, H. | Visse, R. | CA | ZN | Autocatalytic cleavage | Calcium | Collagen | Collagen degradation | Extracellular matrix | Fibroblast collagenase | Glycoprotein | Hydrolase | Inhibitor-free | Matrix metalloproteinases | Metal-binding | Metalloprotease | Polymorphism | Protease | Zinc | Zymogen
