Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
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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. 1999 Jun 4;284(5420):1667-70.
- PubMed ID
- 10356396 [ View in 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.