Fig. 5: FOXO4-DRI and p53^TAD2 synergistically fold upon binding.

a Plot of difference between the secondary ¹³C chemical shifts of Cα and Cβ nuclei of FOXO4-LRI in the absence (black) and presence of 400 µM unlabeled D-p53^TAD2 (orange). b ¹⁵N{¹H}-NOE of 300 µM FOXO4-LRI in the absence (black) and in presence of 400 µM unlabeled D-p53^TAD (orange). Error bars were calculated based on the standard deviation of noise in the saturated and unsaturated spectra and using error propagation. c Ensemble of ten lowest energy structural models of p53^TAD2 (orange) bound to FOXO4-DRI (blue). d Ramachandran plot for residues 47–54 in p53^TAD2 along the different MD simulations of p53^TAD2 alone and in complex with FOXO4-DRI, respectively. e Mean values of RMSD and RMSF of p53^TAD2 and FOXO4-DRI, respectively, in the FOXO4-DRI-p53^TAD2 complex along the different MD simulations. The SD is shown as a shadow. f Structural details of the FOXO4-DRI-p53^TAD2 interaction. Complementary surface charge distributions of p53^TAD2 and key FOXO4-DRI residues involved in the interaction.