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. Author manuscript; available in PMC: 2012 Apr 29.
Published in final edited form as: Structure. 2008 Apr;16(4):643–652. doi: 10.1016/j.str.2008.01.010

Figure 2. The Structural Basis of Histone Recognition by the Bromodomains of PCAF and GCN5.

Figure 2

(A) and (C) Recognition of the acetyl-lysine of H3-K36ac and H3-K9ac peptides by the human PCAF bromodomain, respectively.

(B) and (D) Recognition of amino acid residues flanking the acetyl-lysine of the H3-K36ac and H3-K9ac peptides by the human PCAF bromodomain, respectively.

(E) and (F) Recognition of the acetyl-lysine and its flanking residues of the H4-K16ac peptide by the yeast GCN5 bromodomain (PDB code: 1E6I), respectively.

(G) and (H) Recognition of the acetyl-lysine and its flanking residues of the HIV-1 Tat-K50ac peptide by the human PCAF bromodomain (PDB code: 1JM4), respectively.

In all four structures, side chains of protein or peptide residues are color-coded by atom types—that is, carbon (green for protein and yellow for peptide), oxygen (red), and nitrogen (blue).