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Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition

Tissue inhibitors of metalloproteinases (TIMPs) are natural inhibitors of matrix metalloproteinases (MMPs), enzymes that contribute to cancer and many inflammatory and degenerative diseases. The TIMP N-terminal domain binds and inhibits an MMP catalytic domain, but the role of the TIMP C-terminal do...

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Bibliographische Detailangaben
Veröffentlicht in:J Biol Chem
Hauptverfasser: Raeeszadeh-Sarmazdeh, Maryam, Greene, Kerrie A., Sankaran, Banumathi, Downey, Gregory P., Radisky, Derek C., Radisky, Evette S.
Format: Artigo
Sprache:Inglês
Veröffentlicht: American Society for Biochemistry and Molecular Biology 2019
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Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC6579469/
https://ncbi.nlm.nih.gov/pubmed/31040180
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.008321
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