Figure 1From: Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tailsStructure and molecular contact surfaces of Brd2 BD2. (A) Stereoview of the selected 20 structures of Brd2 BD2, superimposed on backbone atoms (N, C α and C'). (B) Ribbon representation of the average, energy-minimized structure with the secondary structure elements highlighted. The helix nomenclature follows that of hsP/CAF bromodomain [9]. (C) Contact surface emphasized surface hydrophobic potential (left) and surface electrostatic potential (right) at the acetyl-lysine binding site. Yellow denotes hydrophobic potential; red negative potential; and blue positive potential. (D) A clear view of showing the conserved or type conserved side chains lined the hydrophobic cavity, and denoting the negative-charged collar formed by residues D330, D338, D341, D385 and D387. A, B, C and D were produced with MOLMOL or PyMOL.Back to article page