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. Author manuscript; available in PMC: 2014 Nov 27.
Published in final edited form as: J Med Chem. 2013 Nov 11;56(22):9251–9264. doi: 10.1021/jm401334s

Figure 2. Molecular basis of the BRD4 BrD1 recognition of the lead diazobenzene-based BrD inhibitors.

Figure 2

(A) The 3D crystal structure of MS436 (yellow) bound to BRD4-BrD1, depicted in a ribbon diagram. Key amino acid residues at the acetyl-lysine binding site are shown in sticks. The ligand MS436 is color-coded by atom type. (B) Electrostatic surface representation of the BRD4-BrD1 bound to MS436. (C) Superimposition of MS436, MS435 and MS267 when bound to the BRD4-BrD1. Only MS436 bound protein structure is shown. Side chains of the key residues involved in ligand binding are depicted in sticks and color-coded by atom type. The bound water molecules are shown as spheres in magenta. (D), (E), and (F) Schematic diagrams highlighting key interactions in the BRD4 BrD1 recognition of MS436, MS435 and MS267, respectively. Water molecules are shown in magenta spheres, and hydrogen bonds are drawn in dashed line. The figure was generated by using the program LIGPLOT32