2clt
From Proteopedia
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| - | [[Image:2clt.gif|left|200px]]<br /><applet load="2clt" size=" | + | [[Image:2clt.gif|left|200px]]<br /><applet load="2clt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2clt, resolution 2.67Å" /> | caption="2clt, resolution 2.67Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE.'''<br /> | '''CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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] Known structural/functional Site: <scene name='pdbsite=AC1:Zn Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 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 <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ZN:'>ZN</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CLT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:36:44 2008'' |
Revision as of 08:36, 3 February 2008
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CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE.
Contents |
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.
Disease
Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[120353]
About this Structure
2CLT is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Interstitial collagenase, with EC number 3.4.24.7 Known structural/functional Site: . 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
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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
