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...

Descripción completa

Detalles Bibliográficos
Autores principales: Jussupow, Alexander, Lopez, Abraham, Baumgart, Mona, Mader, Sophie L., Sattler, Michael, Kaila, Ville R.I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2022
Materias:
Research Article
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

Internet

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

Ejemplares similares