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. 2018 Jun 22;9:2454. doi: 10.1038/s41467-018-04465-5

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — KBU2046 stabilizes CDC37/HSP90β heterocomplexes. a KBU2046 stabilizes HSP90β/CDC37 heterocomplexes in a DARTS assay. Equimolar amounts of HSP90β and CDC37 protein were pre-incubated with KBU2046, and resultant thermolysin reaction products were detected by silver stain following SDS-PAGE. The mean value (from N = 3 independent experiments) of protein bands indicated by arrows is displayed below each lane, and are expressed as the percentage of untreated control. ANOVA P values for changes in band intensity with concentration are displayed. b In silico model of CDC37 (purple) and HSP90β (gray) depicting KBU2046 hydrogen bonding with Gln119 of HSP90β. c Potential surface of the computed ligand binding pocket of the CDC37/HSP90β model with KBU2046 bound. Atoms within 5 angstroms of KBU2046 are colored by element (carbon, green; nitrogen, blue; oxygen, red). d Potential surface of the whole CDC37/HSP90β dimer (color code: green—HSP90β; gray—CDC37; cyan—Arg167 from CDC37 bisecting the larger pocket and creating a new cleft into which KBU2046 binds)