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Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle

The co-chaperone p23 is a central part of the Hsp90 machinery. It stabilizes the closed conformation of Hsp90, inhibits its ATPase and is important for client maturation. Yet, how this is achieved has remained enigmatic. Here, we show that a tryptophan residue in the proximal region of the tail dece...

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Detalhes bibliográficos
Publicado no:Nat Commun
Main Authors: Biebl, Maximilian M., Lopez, Abraham, Rehn, Alexandra, Freiburger, Lee, Lawatscheck, Jannis, Blank, Birgit, Sattler, Michael, Buchner, Johannes
Formato: Artigo
Idioma:Inglês
Publicado em: Nature Publishing Group UK 2021
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC7864943/
https://ncbi.nlm.nih.gov/pubmed/33547294
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-021-21063-0
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