Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor

Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor

The molecular chaperone Hsp90 oversees the folding of many proteins associated with cancer progression but existing small-molecule inhibitors of this pathway are not isoform-selective. Here, the authors rationally design an Hsp90 inhibitor that displays high selectivity for the Hsp90β isoform.

Bibliographic Details
Main Authors: Anuj Khandelwal, Caitlin N. Kent, Maurie Balch, Shuxia Peng, Sanket J. Mishra, Junpeng Deng, Victor W. Day, Weiya Liu, Chitra Subramanian, Mark Cohen, Jeffery M. Holzbeierlein, Robert Matts, Brian S. J. Blagg
Format: Article
Language:English
Published: Nature Publishing Group 2018-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02013-1

Internet

https://doi.org/10.1038/s41467-017-02013-1

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