Mapping of conformational changes induced upon binding of REV7 to REV3 or CHAMP1 on the crystallography-determined three-dimensional REV7 structures. Chemical shift perturbations (CSPs) were calculated from the 2D [15N,1H]-TROSY-HSQC NMR spectra of apo REV7 and REV7 bound to REV3 ([1], residues 1,8731,898; [2], residues 1,9892,014) or CHAMP1 (residues 328346) polypeptides. For these experiments, the monomeric (KVK), enhanced solubility (YAK) mutant of REV7 was used and the complexes were generated by titrating in the indicated REV3 or CHAMP1 polypeptides (cyan). The REV7 backbone is colored according to the CSP of the corresponding backbone amide, ranging from yellow (CSP = 0 ppm) to red (CSP 0.2 ppm). Backbone regions with unassigned resonances are colored gray.
