Crystal structure of the middle and C-terminal domains of Hsp90α labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target

The 90 kDa heat-shock protein (Hsp90) is an abundant molecular chaperone that is essential to activate, stabilize and regulate the function of a plethora of client proteins. As drug targets for the treatment of cancer and neurodegenerative diseases, Hsp90 inhibitors that bind to the N-terminal ATP-b...

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Detalles Bibliográficos
Autores principales: Peng, Shuxia, Woodruff, Jeff, Pathak, Prabhat Kumar, Matts, Robert L., Deng, Junpeng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2022
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9063849/
https://www.ncbi.nlm.nih.gov/pubmed/35503206
http://dx.doi.org/10.1107/S2059798322002261

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9063849/
https://www.ncbi.nlm.nih.gov/pubmed/35503206
http://dx.doi.org/10.1107/S2059798322002261

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