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Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network
Hsp90 is a molecular chaperone that interacts with a specific set of client proteins and assists their folding. The underlying molecular mechanisms, involving dynamic transitions between open and closed conformations, are still enigmatic. Combining nuclear magnetic resonance, small-angle x-ray scatt...
| Autores principales: | , , , , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
American Association for the Advancement of Science
2021
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8682993/ https://www.ncbi.nlm.nih.gov/pubmed/34919431 http://dx.doi.org/10.1126/sciadv.abl7295 |