Skip to main content
. 2020 Apr 24;11:1972. doi: 10.1038/s41467-020-15879-5

Fig. 2. Structural basis of the asymmetric REV7 conformational dimer.

Fig. 2

a Details of the hydrogen bond network in REV7 dimer interface. Hydrogen bonds are denoted as dashed black lines. b The electrostatic surface representation of the C-REV7-O-REV7 interface (positive potential, blue; negative potential, red). Key basic and acidic residues that interact with each other are shown in sticks. C-REV7 is viewed from O-REV7 along x axis and O-REV7 is viewed from C-REV7 along x axis based on Fig. 2a. In the left panel, C-REV7 is shown as electrostatic surface model and the amino acid residues of O-REV7 that interact with C-REV7 are shown in sticks. In the right panel, O-REV7 is shown in electrostatic surface model while residues of C-REV7 that interact with O-REV7 are shown in sticks. c Structural details of the dimer interface show the contribution of Glu35, Lys44, Lys129 and Lys190 is different between C-REV7 and O-REV7. d, e ITC measurements of binding affinities between REV7E35A-SHLD3(1–82) or REV7K44A-SHLD3(1–82) and REV7K129A. The binding constants (KD values ± standard deviations) and stoichiometries (N) are indicated. KD value and standard deviation were calculated from three independent experiments. Source data are provided as a Source Data file. f, g ITC measurements of the interaction between REV7K129A-SHLD3(1–82) or REV7K190A-SHLD3(1–82) and REV7K129A. REV7K129A-SHLD3(1–82) and REV7K190A-SHLD3(1–82) could hardly bind to REV7K129A. N.D.: no detectable binding.