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Structure of human ...
Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed
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- Morgunova, E (author)
- Karolinska Institutet
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Tuuttila, A (author)
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Bergmann, U (author)
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Isupov, M (author)
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- Lindqvist, Y (author)
- Karolinska Institutet
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- Schneider, G (author)
- Karolinska Institutet
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- Tryggvason, K (author)
- Karolinska Institutet
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(creator_code:org_t)
- American Association for the Advancement of Science (AAAS), 1999
- 1999
- English.
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In: Science (New York, N.Y.). - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 284:5420, s. 1667-1670
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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 and Content Type
- ref (subject category)
- art (subject category)
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