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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...
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| 主要な著者: | , , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2011
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| 主題: | |
| オンライン･アクセス: | 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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