1. Structure of the BRCT Repeats of BRCA1 Bound to a BACH1 Phosphopeptide
Eric N. Shiozaki, Lichuan Gu, Nieng Yan, Yigong Shi 
Molecular Cell 
Volume 14, Issue 3, Pages (May 2004)
DOI: /S (04)

2. Figure 1
Overall Structure of the BRCT Repeats of Human BRCA1 Bound to a Phosphorylated BACH1 Peptide
(A) Schematic representation of the BRCT-BACH1 complex. The two tandem BRCT repeats are colored blue and green, respectively. The structural elements between the two BRCT repeats are shown in orange. The bound BACH1 peptide is colored magenta. Phe993 and the phosphorylated Ser990 of the BACH1 peptide are highlighted.
(B) The phosphorylated BACH1 peptide binds to a highly conserved surface cleft among BRCA1 proteins across species. The BRCT repeats are shown in a surface representation. Residues that are invariant in all four BRCA1 orthologs across species (human, rat, chicken, and fish) are highlighted in red, while residues that are completely divergent are shown in white. The bound BACH1 peptide is shown in green.
(C) Two amino acids in the BACH1 peptide, pSer990 and Phe993, make dominant contributions to the binding of the BRCA1 BRCT repeats. The contribution of individual BACH1 amino acids is indicated below the sequences. Hydrogen bonds to the side chains and backbone groups are represented by red and green triangles, respectively; van der Waals contacts are shown by blue squares. (C) and (A) were generated using GRASP (Nicholls et al., 1991). All other figures were made using MOLSCRIPT (Kraulis, 1991).
Molecular Cell  , DOI: ( /S (04) )

3. Figure 2
Specific Recognition of the Phosphorylated BACH1 Peptide by the BRCT Repeats of BRCA1
(A) Stereo view of the BRCT-BACH1 interface. The two tandem BRCT repeats are colored blue and green. The bound BACH1 peptide is shown in magenta. Hydrogen bonds are represented by red dashed lines. Oxygen and nitrogen atoms are shown as red and blue balls, respectively.
(B) Sequence alignment of BRCA1 orthologs from human, mouse, chicken, and fish. Color choices for the two BRCT motifs are the same as in Figure 1A. Conserved residues are highlighted in yellow. Hydrogen bonds to the side chains and backbone groups are indicated below the sequences by red and green triangles, respectively; van der Waals contacts are shown by blue squares. Residues that were targeted for missense mutations in at least five breast cancer patients are identified by red columns above the sequences, with the height of the column corresponding to the number of mutations.
Molecular Cell  , DOI: ( /S (04) )

4. Figure 3
The BRCT-BACH1 Interaction Is Frequently Targeted for Inactivation in Breast Cancers
(A) The conserved surface cleft of the BRCT repeats is most frequently targeted for mutations. Cancer-derived missense mutations in the BRCT repeats of BRCA1 were mapped onto the surface of the structure, with different frequencies encoded by distinct colors. Two of the most prevalent mutations, Met1775Arg and Arg1699Ala, affect residues in the surface cleft that make critical interactions to the phosphorylated BACH1 peptide.
(B) Tumor-derived mutations in BRCA1 result in significantly weakened interactions with the phosphorylated BACH1 peptide. Representative ITC results are shown between the phosphorylated BACH1 peptide and the BRCT repeats of BRCA1.
Molecular Cell  , DOI: ( /S (04) )

5. Figure 4
Conserved Recognition of Phosphoserine by the BRCT Repeats from Other Proteins Involved in DNA Damage and Repair Response
(A) A surface representation of the BRCT repeats of BRCA1. Residues that are invariant in all four proteins are shown in dark blue, while residues that are completely divergent are shown in white. The bound BACH1 peptide is shown in magenta.
(B) BRCA1 residues that coordinate phosphoserine 990 (pSer990) of BACH1 are conserved in BARD1, MDC1, and 53BP1. In contrast, BRCA1 residues that interact with Phe993 of BACH1 are not conserved. The secondary structural elements are indicated below the sequence alignment to highlight the finding that pSer990 of BACH1 is exclusively coordinated by the N-terminal BRCT motif whereas Phe993 is primarily bound by residues in the C-terminal BRCT motif.
Molecular Cell  , DOI: ( /S (04) )