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Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast

Hsp90 is a highly conserved molecular chaperone important for the activity of many client proteins. Hsp90 has an N-terminal ATPase domain (N), a middle domain (M) that interacts with clients and a C-terminal dimerization domain (C). “Closing” of dimers around clients is regulated by ATP binding, co-...

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Detalles Bibliográficos
Publicado en:J Mol Biol
Autores principales: Reidy, Michael, Masison, Daniel C.
Formato: Artigo
Lenguaje:Inglês
Publicado: 2020
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC7437358/
https://ncbi.nlm.nih.gov/pubmed/32565117
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2020.06.015
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