Fig. 2: Structure of the JNK1-ATF2 complex.

a Interaction region mapping by NMR. ¹⁵N-labeled ATF2(19-78) was mixed with JNK1 in two different molar ratio, and intensity changes, normalized to the peak intensity without JNK1, for ATF2 ¹H-¹⁵N HSQC peaks for the 0.5:1 (black) or 1:1 (red) JNK1:ATF2 experiment were plotted. ‘x’ indicates resonances of residues which are not resolved in the spectra and, therefore, could not be quantified or prolines. b Analysis of the JNK-ATF2(Zn-finger) protein–protein binding interface based on the HADDOCK model. Amino acid residues lying at the interface (Q34, V44, H47, and K48) were mutated to alanine, glutamate or arginine. The binding affinity of mutant ATF2(19–100) constructs (mut) were compared to that of the wild-type (wt) (Supplementary Fig. 4). The panels on the right show the summary of competitive fluorescence polarization based protein–protein binding assay results on top and the competitive binding curves for the wild-type (black) and for the Q34R/H47R double mutant (red) below. Error bars on the binding isotherms show SD based on three independent measurements (n = 3). Date are represented as mean values ± SD. c Crystal structure of the JNK1-ATF2(19–58) complex. The left panel shows the superposition of the HADDOCK model (black) with the crystal structure (yellow+cyan; the RMSD of Cα atoms for the ATF2(24-55) region using JNK as the reference, was 0.9 Å). Panels on the right show zoomed-in views at the CD-groove highlighting K48 (top) or at the hydrophobic groove highlighting M51, L53, and F55 (bottom) from the ATF2 D-motif. The simulated annealing Fo-Fc omit map of ATF2 is shown at 1.5ϭ. Source data are provided as a Source data file.