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.
Publication types
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Comment
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Catalytic Domain
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Enzyme Activation
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Enzyme Precursors / chemistry*
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Enzyme Precursors / metabolism
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Fibronectins / chemistry
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Gelatinases / chemistry*
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Gelatinases / metabolism
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Hemopexin / chemistry
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Humans
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Hydrogen Bonding
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Matrix Metalloproteinase 2
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Metalloendopeptidases / chemistry*
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Metalloendopeptidases / metabolism
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
Substances
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Enzyme Precursors
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Fibronectins
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Hemopexin
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Gelatinases
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Metalloendopeptidases
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Matrix Metalloproteinase 2