Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1

Complex conformational dynamics are essential for function of the dimeric molecular chaperone heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization that is necessary to attain ATPase competence. The intrinsic, but weak, ATP hydrolyzing activity of human Hsp90 is marked...

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Detalles Bibliográficos
Autores principales: Xu, Wanping, Beebe, Kristin, Chavez, Juan D., Boysen, Marta, Lu, YinYing, Zuehlke, Abbey D., Keramisanou, Dimitra, Trepel, Jane B., Prodromou, Christosomos, Mayer, Matthias P., Bruce, James E., Gelis, Ioannis, Neckers, Len
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6561935/
https://www.ncbi.nlm.nih.gov/pubmed/31189925
http://dx.doi.org/10.1038/s41467-019-10463-y

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6561935/
https://www.ncbi.nlm.nih.gov/pubmed/31189925
http://dx.doi.org/10.1038/s41467-019-10463-y

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