1CK7
GELATINASE A (FULL-LENGTH)
Summary for 1CK7
| Entry DOI | 10.2210/pdb1ck7/pdb |
| NMR Information | BMRB: 5262 |
| Descriptor | PROTEIN (GELATINASE A), ZINC ION, CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | hydrolase (metalloprotease), full-length, metalloproteinase, gelatinase a, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Secreted, extracellular space, extracellular matrix. Isoform 2: Cytoplasm: P08253 |
| Total number of polymer chains | 1 |
| Total formula weight | 71497.03 |
| Authors | Morgunova, E.,Tuuttila, A.,Bergmann, U.,Isupov, M.,Lindqvist, Y.,Schneider, G.,Tryggvason, K. (deposition date: 1999-04-28, release date: 1999-08-25, Last modification date: 2024-11-13) |
| Primary citation | Morgunova, E.,Tuuttila, A.,Bergmann, U.,Isupov, M.,Lindqvist, Y.,Schneider, G.,Tryggvason, K. Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. Science, 284:1667-1670, 1999 Cited by PubMed Abstract: Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability. PubMed: 10356396DOI: 10.1126/science.284.5420.1667 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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