2j0t
From Proteopedia
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CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-1 IN COMPLEX WITH THE INHIBITORY DOMAIN OF TIMP-1
Overview
The mammalian collagenases are a subgroup of the matrix metalloproteinases, (MMPs) that are uniquely able to cleave triple helical fibrillar, collagens. Collagen breakdown is an essential part of extracellular matrix, turnover in key physiological processes including morphogenesis and wound, healing; however, unregulated collagenolysis is linked to important, diseases such as arthritis and cancer. The tissue inhibitors of, metalloproteinases (TIMPs) function in controlling the activity of MMPs, including collagenases. We report here the structure of a complex of the, catalytic domain of fibroblast collagenase (MMP-1) with the N-terminal, inhibitory domain of human TIMP-1 (N-TIMP-1) at 2.54 A resolution., Comparison with the previously reported structure of the, TIMP-1/stromelysin-1 ... [(full description)]
About this Structure
2J0T is a [Protein complex] structure of sequences from [Homo sapiens] with ZN and CA 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 the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1., Iyer S, Wei S, Brew K, Acharya KR, J Biol Chem. 2007 Jan 5;282(1):364-71. Epub 2006 Oct 18. PMID:17050530
Page seeded by OCA on Tue Oct 30 11:55:00 2007
Categories: Homo sapiens | Interstitial collagenase | Protein complex | Acharya, K.R. | Brew, K. | Iyer, S. | Wei, S. | CA | ZN | Autocatalytic cleavage | Calcium | Collagen degradation | Collagenase | Erythrocyte maturation | Extracellular matrix | Glycoprotein | Hydrolase | Matrix metalloprotease | Metal-binding | Metalloenzyme inhibitor | Metalloprotease | Metalloprotease inhibitor | Ob fold | Polymorphism | Protease | Tissue inhibitor of metalloproteinase | Zinc | Zymogen
