Fig. 2: RIF1-L phospho-SPKF peptide binds to tandem BRCT domains of BRCA1 in vitro. | Nature Communications

Fig. 2: RIF1-L phospho-SPKF peptide binds to tandem BRCT domains of BRCA1 in vitro.

From: The human RIF1-Long isoform interacts with BRCA1 to promote recombinational fork repair under DNA replication stress

Fig. 2

A, B Fluorescence polarisation analysis of binding affinities between BRCA1-BRCT domain and RIF1-L phospho-peptide with indicated treatment or mutations. Source data are provided as a Source Data file. C Crystal structure of RIF1-L phospho-peptide (stick presentation) in complex with BRCA1-BRCT domain (space-filling presentation), solved by X-ray diffraction. The phosphorus atom is represented in orange. Residues on RIF1-L phospho-peptide are labelled with pink text (S2265, K2267, F2268, K2269). Residue on BRCA-BRCT domain is labelled with green text (E1698). D Model of RIF1-L interaction with BRCA1. In RIF1-L protein presentation, purple bards indicate PP1-interacting motifs; pink box indicates Exon 31; red bar indicates the S2265PKF motif. RIF1-L phosphoS2265PKF motif binds to the C-terminal tandem BRCT domains of BRCA1.

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