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Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast
Hsp90 is a highly conserved molecular chaperone important for the activity of many client proteins. Hsp90 has an N-terminal ATPase domain (N), a middle domain (M) that interacts with clients and a C-terminal dimerization domain (C). “Closing” of dimers around clients is regulated by ATP binding, co-...
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| Gepubliceerd in: | J Mol Biol |
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| Hoofdauteurs: | , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2020
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7437358/ https://ncbi.nlm.nih.gov/pubmed/32565117 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2020.06.015 |
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