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. 2022 Jan 7;12:116. doi: 10.1038/s41598-021-04099-6

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Binding interfaces in the simulated PEA-15/ERK2 complex. PEA-15 is shown in cyan and ERK2 in magenta. Interface residues on PEA-15 are colored in dark blue, and residues on ERK2 are colored in red. (A) The interface between PEA-15 DED and ERK2 DEF docking site. PEA-15 interacts with ERK2 with its helices α5/α6, including direct interaction between PEA-15 R71 and ERK2 Y205, consistent with crystal structure 4IZ5. (B) Interface between PEA-15 C-terminal tail and ERK2 D-peptide binding site, including interactions between PEA-15 K128 and ERK2 D124 and PEA-15 K129 and ERK2 D318. Another interaction that can be observed is between PEA-15 D110 and ERK2 R225. There are no direct interactions between either phosphorylation sites, S104 and S116, and ERK2 residues. The molecular structures were visualized and generated using PyMOL version 2.4 (http://www.pymol.org/).