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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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The simulated complex structure of PEA-15pp/FADD. (A) PEA-15pp in the complex (orange) is superimposed with free-form PEA-15pp (magenta) with the RMSD of 0.803 Å before the kink on helix α6. There is no significant conformational change between the free and bound forms. (B) FADD in the complex (yellow) is superimposed with the NMR structure of intact FADD, 2GF5 (magenta), over DED residues (RMSD 2.118 Å). PEA-15pp in the complex is colored cyan. DED–DED interaction in the complex is orthogonal in directions. The FADD DD in the complex rotated about 90° from the free form around the linker between the two domains. (C) same as (B) but observed from the top of FADD DD to illustrate the relative positions of the six helices on DD. PEA-15pp is not shown for clarity. The molecular structures were visualized and generated using PyMOL version 2.4 (http://www.pymol.org/).