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. Author manuscript; available in PMC: 2021 Apr 15.
Published in final edited form as: J Mol Biol. 2019 Oct 15;432(6):1624–1639. doi: 10.1016/j.jmb.2019.10.007

Figure 3. Binding of MTA1 and FOG1 to RBBP4.

Figure 3.

A cartoon diagram depicts an overlay of crystal structures showing RBBP4 bound to four different peptides. Two different peptides from MTA1 (amino acids 462–546 in yellow and 670–695 in cyan; PDB ID: 5FXY and 4PBZ, respectively) bind RBBP4 (green) through a common interface. Likewise, the N-terminal helix from histone H4 (amino acids 24–41 in blue; PDB ID: 3CFV) binds to the same region of RBBP4. In contrast, the N-terminal FOG1 peptide (amino acids 1–15 in magenta; PDB ID: 2XU7) binds to a distinct region of RBBP4 that does not overlap with the binding surfaces for MTA1 or histone H4. Note that MTA1 residues not observed in the crystal structure (519–528) are indicated with a yellow dashed line.