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. 2023 Jun 19;14:3543. doi: 10.1038/s41467-023-38864-0

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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. 3 — a Cartoon depicting primary and secondary interactions within a 14-3-3/client complex. b PEAK3 binding to the amphipathic grooves of 14-3-3ε and 14-3-3β, highlighting key conserved interactions. c Known binding modes of 14-3-3/client complexes found in the Protein Data Bank. 14-3-3 monomers are shown in green and light green, 14-3-3 substrate monomers are shown in pink and light pink, and phosphorylated residues or phosphomimetics which engage the 14-3-3 binding grooves are shown as red spheres. See Methods for alignment details. d PEAK3/14-3-3 structure highlighting PEAK3 SHED domain (box e) and pseudokinase domain (box f-h) interactions with 14-3-3ε. e-h Zoomed-in view of PEAK3/14-3-3ε secondary interface, highlighting key interactions. Dashed lines in red indicate interactions with distances ≤ 4 Å.