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. 2018 Jan 17;9:265. doi: 10.1038/s41467-017-02711-w

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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. 6 — Interaction of a pY298 phosphopeptide with the SH2 domains of Yes and other nRTKs. a ITC isotherms for the interaction of pYESL with the SH2 domains of Yes, Src, Hck, and Lyn (left), together with the enthalpic and entropic contributions to the free energy change (middle) and the corresponding K_d values (right). Error bars in the K_d values correspond to the errors resulted in fitting of the data into a single binding site model. b Overlay of the ¹⁵N-HSQC of Yes^SH2 in the absence (black) and presence (green) of one equivalent of pYESL. c CSP as a function of Yes^SH2 primary sequence. The mean and one standard deviation above the mean are marked by solid and broken lines, respectively. d Mapping of the observed CSPs on the structure of SH2. The black broken line highlights the peptide-binding site as identified in other SH2 domains. e The effect of competing concentrations of SH2^Yes or pYESL (at 0.5 mM) on the overall phosphorylation levels of Hsp90 in the context of ternary complexes formed with bRaf and Y4F/Y298F (lane 1) or wild-type Cdc37 (lanes 2–4), monitored by staining with Pro-Q Diamond (top) and coomassie (bottom)