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...

Descripción completa

Detalles Bibliográficos
Autores principales: Biebl, Maximilian M., Lopez, Abraham, Rehn, Alexandra, Freiburger, Lee, Lawatscheck, Jannis, Blank, Birgit, Sattler, Michael, Buchner, Johannes
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7864943/
https://www.ncbi.nlm.nih.gov/pubmed/33547294
http://dx.doi.org/10.1038/s41467-021-21063-0

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7864943/
https://www.ncbi.nlm.nih.gov/pubmed/33547294
http://dx.doi.org/10.1038/s41467-021-21063-0

Ejemplares similares