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dc.contributor.authorMatts, Robert L.
dc.contributor.authorDixit, Anshuman
dc.contributor.authorPeterson, Laura B.
dc.contributor.authorSun, Liang
dc.contributor.authorVoruganti, Sudhakar
dc.contributor.authorKalyanaraman, Palgunan
dc.contributor.authorHartson, Steve D.
dc.contributor.authorVerkhivker, Gennady M.
dc.contributor.authorBlagg, Brian S. J.
dc.date.accessioned2017-03-30T17:49:33Z
dc.date.available2017-03-30T17:49:33Z
dc.date.issued2011-08-19
dc.identifier.citationMatts, 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/cb200052xen_US
dc.identifier.urihttp://hdl.handle.net/1808/23521
dc.description.abstractThe 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.en_US
dc.publisherACS Chem Biol.en_US
dc.rightsCopyright © 2011 American Chemical Societyen_US
dc.titleElucidation of the Hsp90 C-terminal Inhibitor Binding Siteen_US
dc.typeArticleen_US
kusw.kuauthorDixit, Anshuman
kusw.kuauthorPeterson, Laura B.
kusw.kuauthorBlagg, Brian S. J.
kusw.kudepartmentBiochemistry and Molecular Biologyen_US
kusw.kudepartmentMedicinal Chemistryen_US
dc.identifier.doi10.1021/cb200052xen_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.rights.accessrightsopenAccess


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