Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed
E Morgunova, A Tuuttila, U Bergmann, M Isupov… - Science, 1999 - science.org
Science, 1999•science.org
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.
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.
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.
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