Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed
- 4 June 1999
- journal article
- editorial
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 284 (5420), 1667-1670
- https://doi.org/10.1126/science.284.5420.1667
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.Keywords
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