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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Detalhes bibliográficos
Publicado no:J Biol Chem
Main Authors: Raeeszadeh-Sarmazdeh, Maryam, Greene, Kerrie A., Sankaran, Banumathi, Downey, Gregory P., Radisky, Derek C., Radisky, Evette S.
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2019
Assuntos:
Protein Structure and Folding
Acesso em linha: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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