Fig. 3: The highly conserved FXPWFP motif of SHLD3 binds to C-REV7 and enhances the binding affinity between C-REV7 and O-REV7.
From: Molecular basis for assembly of the shieldin complex and its implications for NHEJ
a The interface between SHLD3 and C-REV7. C-REV7 and O-REV7 are shown in electrostatic surface representation (positive potential, blue; negative potential, red), SHLD3 in ribbon view, and the FXPWFP motif in sticks. The N terminus of SHLD3 is also indicated. Residues 1-37 of SHLD3 are shown in ribbon. b Close-up view of the interface between the FXPWFP motif (magenta) and C-REV7 (green), O-REV7 (cyan). Hydrogen bonds are indicated by dashed lines and the residues that are involved in the hydrophobic interactions are shown in sticks. c–e ITC measurements of interaction between distinct REV7K44A-SHLD3(1–82) truncations or mutants and REV7K129A. The calculated N and KD are indicated as described in Fig. 2d. Source data are provided as a Source Data file.
