Local unfolding of the HSP27 monomer regulates chaperone activity

The small heat-shock protein HSP27 is a redox-sensitive molecular chaperone that is expressed throughout the human body. Here, we describe redox-induced changes to the structure, dynamics, and function of HSP27 and its conserved α-crystallin domain (ACD). While HSP27 assembles into oligomers, we sho...

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Detalles Bibliográficos
Autores principales: Alderson, T. Reid, Roche, Julien, Gastall, Heidi Y., Dias, David M., Pritišanac, Iva, Ying, Jinfa, Bax, Ad, Benesch, Justin L. P., Baldwin, Andrew J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6403371/
https://www.ncbi.nlm.nih.gov/pubmed/30842409
http://dx.doi.org/10.1038/s41467-019-08557-8

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6403371/
https://www.ncbi.nlm.nih.gov/pubmed/30842409
http://dx.doi.org/10.1038/s41467-019-08557-8

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