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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Dettagli Bibliografici
Pubblicato in:J Biol Chem
Autori principali: Raeeszadeh-Sarmazdeh, Maryam, Greene, Kerrie A., Sankaran, Banumathi, Downey, Gregory P., Radisky, Derek C., Radisky, Evette S.
Natura: Artigo
Lingua:Inglês
Pubblicazione: American Society for Biochemistry and Molecular Biology 2019
Soggetti:
Protein Structure and Folding
Accesso online: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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