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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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| 出版年: | Nat Commun |
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| 主要な著者: | , , , , , , , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Nature Publishing Group UK
2019
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6561935/ https://ncbi.nlm.nih.gov/pubmed/31189925 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-019-10463-y |
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