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. 2021 Jun 17;28(6):835–847.e5. doi: 10.1016/j.chembiol.2021.02.006

Figure 1.

Figure 1

RAD51 interaction with BRC4

(A) Structure of RAD51 ATPase domain (surface) with BRC4 repeat of BRCA2 with FxxA binding motif colored green and the LFDE-motif in blue (PDB: 1n0w).

(B) Structure of oligomeric RAD51 with oligomerization epitope (orange) of one protomer binding the next molecule in the filament (surface) (PDB: 5nwl).

(C) Sequences of BRC4 repeat, and its FxxA and LFDE epitopes containing half peptides and the isolated RAD51 oligomerization peptide (OP).

(D) Competitive FP assay with labeled BRC4 repeat as probe which shows competitive binding to ChimRAD51 protein with the two BRC4 half-peptides (FxxA and LFDE, green and blue) and RAD51 oligomerization peptide (OP, orange). The dissociation constants measured for the FxxA half-peptide and for the oligomerization peptides were 36 ± 7 μM and 18 ± 3 μM, respectively.