Fig. 4: Crystal structure explains the effect of human SNP variants on HSF2BP-BRCA2 interaction.

a 3D view of the ARM chain D in complex with motif 1 of BRCA2 F15X chain F. The ARM and BRCA2 protein fragments are displayed as gray and black ribbons, respectively. The side chains substituted for coimmunoprecipitation studies are displayed in sticks, and colored as in Fig. 1a (red: no binding; blue: residual binding with the residue name underlined when wild-type binding was observed). b Zoom views on residues forming a hydrogen bond network between ARM and BRCA2 F15X. Asparagine side chains from ARM interact with backbone atoms from BRCA2 F15X. The side chains of BRCA2 are not displayed; consistently, the BRCA2 residue names are in brackets. Hydrogens were added to the crystal structure for clarity. c 3D view of the ARM chains B and D in complex with the BRCA2 F15X chain F. The ARM and BRCA2 protein fragments, as well as the mutated side chains, are displayed as in a, except that full labels are shown for BRCA2 residues. d Zoom views on BRCA2 F15X mutations P to L and their interacting residues in ARM chains B and D. Residues marked in italics have not been mutated in our study.