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Elucidation of the Hsp90 C-terminal Inhibitor Binding Site
Matts, Robert L. Dixit, Anshuman Peterson, Laura B. Sun, Liang Voruganti, Sudhakar Kalyanaraman, Palgunan Hartson, Steve D. Verkhivker, Gennady M. Blagg, Brian S. J.
Matts, Robert L.
Dixit, Anshuman
Peterson, Laura B.
Sun, Liang
Voruganti, Sudhakar
Kalyanaraman, Palgunan
Hartson, Steve D.
Verkhivker, Gennady M.
Blagg, Brian S. J.
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Abstract
The Hsp90 chaperone machine is required for the folding, activation and/or stabilization of more than 50 proteins directly related to malignant progression. Hsp90 contains small molecule binding sites at both its N- and C-terminal domains, however, limited structural and biochemical data regarding the C-terminal binding site is available. In this report, the small molecule binding site in
the Hsp90 C-terminal domain was revealed by protease fingerprinting and photoaffinity labeling utilizing LC-MS/MS. The identified site was characterized by generation of a homology model for hHsp90α using the SAXS open structure of HtpG and docking the bioactive conformation of NB into the generated model. The resulting model for the bioactive conformation of NB bound to Hsp90α is presented herein.
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2011-08-19
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ACS Chem Biol.
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Matts, R. L., Dixit, A., Peterson, L. B., Sun, L., Voruganti, S., Kalyanaraman, P., … Blagg, B. S. J. (2011). Elucidation of the Hsp90 C-terminal Inhibitor Binding Site. ACS Chemical Biology, 6(8), 800–807. http://doi.org/10.1021/cb200052x