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. 2023 Jun 19;14:3542. doi: 10.1038/s41467-023-38869-9

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© The Author(s) 2023

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 — a Binding of PEAK3^tandem-pS69 (left) and PEAK3^tandem-S69 peptides (right) to 14-3-3ɣ as measured by SPR. b Overall structure of 14-3-3ε: PEAK3^tandem-pS69 peptide showing 14-3-3 dimer antiparallel arrangement with each monomer (pink cartoon/surface) bound to a single copy of the PEAK3^tandem-pS69 peptide (yellow sticks). Chain A of 14-3-3ε is in dark pink and chain B is in light pink. c Zoom in highlighting peptide groove and showing the central pS69 residue of the PEAK3 phosphopeptide interacting with K50, R57, Y131 and R130. d Unbiased Fo-Fc omit map (green mesh, contoured at 3.0σ) showing peptide density prior to modeling and final modeled PEAK3^tandem-pS69 phosphopeptide (yellow sticks). e Superposition of the peptide modeled in each 14-3-3 monomer (chains A–D, sticks) in the asymmetric unit.