2clt
CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE.
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OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[120353]
About this StructureAbout 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 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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