Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells

Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells

The interaction between the HSP90 chaperone and its client kinases is sensitive to the conformational status of the kinase, and stabilization of the kinase fold by small molecules strongly decreases chaperone interaction. Here we exploit this observation and assay small-molecule binding to kinases i...

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Bibliographic Details
Main Authors: Taipale, Mikko (Contributor), Krykbaeva, Irina (Contributor), Whitesell, Luke (Contributor), Santagata, Sandro (Contributor), Zhang, Jianming (Author), Liu, Qingsong (Author), Gray, Nathanael S. (Author), Lindquist, Susan (Contributor)
Other Authors: Massachusetts Institute of Technology. Department of Biology (Contributor), Whitehead Institute for Biomedical Research (Contributor)
Format: Article
Language:English
Published: Nature Publishing Group, 2014-02-14T16:43:32Z.
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