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. 2020 Aug 13;10:13686. doi: 10.1038/s41598-020-70721-8

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© The Author(s) 2020

Open AccessThis 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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Comparison of structure and activity of wt and 3CX mutant forms of rP75NTR. (A) Secondary chemical shifts of C_α nuclei of rP75-ΔECD (blue bars) and rP75-ΔECD-3CX (red bars). The secondary structure of the death domain, according to PDB ID 1NGR is shown on top. (B) The propensity of ɑ-helical conformation, according to the TALOS-N prediction, based on NMR chemical shifts of rP75-ΔECD (blue bars) and rP75-ΔECD-3CX (red bars). (C) Overlay of ¹H,¹⁵N-TROSY-HSQC spectra (glycine regions) of rP75-ΔECD (blue) and rP75-ΔECD-3CX (red). The assignment is provided in black and red (for the mutated S379 residue). (D) Binding of TRAF6 to wild type and mutant rP75-3CX in transfected HEK293 cells. Full-length blots are presented in Supplementary Fig S8. The figure was prepared using the program Inkscape 0.92 (https://inkscape.org/).