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...

Descripción completa

Detalles Bibliográficos
Autores principales: Lopez, Abraham, Dahiya, Vinay, Delhommel, Florent, Freiburger, Lee, Stehle, Ralf, Asami, Sam, Rutz, Daniel, Blair, Laura, Buchner, Johannes, Sattler, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2021
Materias:
Biomedicine and Life Sciences
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

Internet

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

Ejemplares similares