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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5420
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pubmed:dateCreated |
1999-6-22
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1667-70
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:10356396-Amino Acid Sequence,
pubmed-meshheading:10356396-Catalytic Domain,
pubmed-meshheading:10356396-Enzyme Activation,
pubmed-meshheading:10356396-Enzyme Precursors,
pubmed-meshheading:10356396-Fibronectins,
pubmed-meshheading:10356396-Gelatinases,
pubmed-meshheading:10356396-Hemopexin,
pubmed-meshheading:10356396-Humans,
pubmed-meshheading:10356396-Hydrogen Bonding,
pubmed-meshheading:10356396-Matrix Metalloproteinase 2,
pubmed-meshheading:10356396-Metalloendopeptidases,
pubmed-meshheading:10356396-Models, Molecular,
pubmed-meshheading:10356396-Molecular Sequence Data,
pubmed-meshheading:10356396-Protein Conformation,
pubmed-meshheading:10356396-Protein Folding,
pubmed-meshheading:10356396-Protein Structure, Secondary
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pubmed:year |
1999
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pubmed:articleTitle |
Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
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pubmed:affiliation |
Division of Matrix Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Comment,
Research Support, Non-U.S. Gov't
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