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Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex
Hsp90 is an essential molecular chaperone required for the folding and activation of many hundreds of cellular “client” proteins. The ATP-dependent chaperone cycle involves significant conformational rearrangements of the Hsp90 dimer and interaction with a network of cochaperone proteins. Little is...
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| Auteurs principaux: | , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
2011
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3144320/ https://ncbi.nlm.nih.gov/pubmed/21700222 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2011.04.023 |
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