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. 2017 Aug 14;7:8057. doi: 10.1038/s41598-017-08303-4

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© The Author(s) 2017

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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(A) The CAS SH3 binding motif based on the 14 unique sequences obtained from phage display. The x-axis shows the residue position relative to proline (position 0)^64–66. (B) The CAS SH3 domain binding interaction partners with their respective binding motifs. Interactors with small differences in binding motif are in italics. References (^R) are superscripted. (C–E) Isothermal titration calorimetry (ITC) data obtained for the interaction of CAS SH3 with four synthetic peptides.