CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE.

File:2clt.gif


2clt, resolution 2.67Å

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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, ... [(full description)]

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]. Structure known Active Site: AC1. 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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