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The client protein p53 forms a molten globule-like state in the presence of Hsp90

It is not currently known in what state (folded, unfolded, alternatively folded) client proteins interact with chaperone Hsp90. We show that one client, the p53 DNA-binding domain, undergoes a structural change in the presence of Hsp90 to adopt a molten globule-like state. Addition of one- and two-d...

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Detalles Bibliográficos
Autores principales: Park, Sung Jean, Borin, Brendan N., Martinez-Yamout, Maria A., Dyson, H. Jane
Formato: Texto
Lenguaje:English
Publicado: 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087862/
https://www.ncbi.nlm.nih.gov/pubmed/21460846
http://dx.doi.org/10.1038/nsmb.2045