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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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Key interactions between the PTP-PEST- and Vinculin- derived peptides and CAS SH3 domain. (A) PTP-PEST- and (B) Vinculin-derived peptides are shown in stick representation. The CAS SH3 parts of the complexes are shown by electrostatic potential surface representation (APBS). Four binding pockets are highlighted with rectangles (orange - zero pocket/upstream SDE, green - 1st pocket, blue - 2nd pocket, yellow - 3rd pocket), and the interaction interface is shown on the right in detail (PTP-PEST in cyan, Vinculin in green, CAS SH3 in gray). Capital letters E/D, P, K, L/R represent the key ligand amino acid residue in each CAS SH3 binding pocket. The distances between a pair of residues involved in hydrophobic interaction are shown in pink; hydrogen bonds are represented by black dotted lines.