A switch point in the molecular chaperone Hsp90 responding to client interaction

Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that undergoes large conformational changes during its functional cycle. It has been established that conformational switch points exist in the N-terminal (Hsp90-N) and C-terminal (Hsp90-C) domains of Hsp90, however information for switc...

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Detalles Bibliográficos
Autores principales: Rutz, Daniel Andreas, Luo, Qi, Freiburger, Lee, Madl, Tobias, Kaila, Ville R. I., Sattler, Michael, Buchner, Johannes
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5902578/
https://www.ncbi.nlm.nih.gov/pubmed/29662162
http://dx.doi.org/10.1038/s41467-018-03946-x

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5902578/
https://www.ncbi.nlm.nih.gov/pubmed/29662162
http://dx.doi.org/10.1038/s41467-018-03946-x

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