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Cross monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity

The ubiquitous molecular chaperone Hsp90 plays a critical role in substrate protein folding and maintenance, but the functional mechanism has been difficult to elucidate. In previous work a model Hsp90 substrate revealed an activation process in which substrate binding accelerates a large open/close...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Päätekijät: Street, Timothy O., Lavery, Laura A., Verba, Kliment, Lee, Chung-Tien, Mayer, Matthias P., Agard, David A.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2011
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC3282117/
https://ncbi.nlm.nih.gov/pubmed/22063096
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2011.10.038
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