2CLT
Crystal structure of the active form (full-length) of human fibroblast collagenase.
Summary for 2CLT
| Entry DOI | 10.2210/pdb2clt/pdb |
| Related | 1AYK 1CGE 1CGF 1CGL 1HFC 1SU3 2AYK 2TCL 3AYK 4AYK 966C |
| Descriptor | INTERSTITIAL COLLAGENASE, CALCIUM ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | extracellular matrix, fibroblast collagenase, zinc, calcium, zymogen, protease, collagen, autocatalytic cleavage, matrix metalloproteinases, hydrolase, polymorphism, glycoprotein, metal-binding, inhibitor-free, metalloprotease, collagen degradation |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Secreted, extracellular space, extracellular matrix (Probable): P03956 |
| Total number of polymer chains | 2 |
| Total formula weight | 85042.40 |
| Authors | Iyer, S.,Visse, R.,Nagase, H.,Acharya, K.R. (deposition date: 2006-04-29, release date: 2006-08-09, Last modification date: 2024-11-06) |
| Primary citation | Iyer, S.,Visse, R.,Nagase, H.,Acharya, K.R. Crystal Structure of an Active Form of Human Mmp-1. J.Mol.Biol., 362:78-, 2006 Cited by PubMed Abstract: 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. PubMed: 16890240DOI: 10.1016/J.JMB.2006.06.079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.67 Å) |
Structure validation
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