Cargando…
Extended conformational states dominate the Hsp90 chaperone dynamics
The heat shock protein 90 (Hsp90) is a molecular chaperone central to client protein folding and maturation in eukaryotic cells. During its chaperone cycle, Hsp90 undergoes ATPase-coupled large-scale conformational changes between open and closed states, where the N-terminal and middle domains of th...
| Autores principales: | , , , , , |
|---|---|
| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2022
|
| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9251789/ https://www.ncbi.nlm.nih.gov/pubmed/35667441 http://dx.doi.org/10.1016/j.jbc.2022.102101 |