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. Author manuscript; available in PMC: 2015 Dec 24.
Published in final edited form as: Nature. 2006 May 21;442(7098):91–95. doi: 10.1038/nature04802

Figure 3. Details of the intermolecular contacts in the H3(1–15)K4me3 peptide–BPTF PHD finger complex and comparison with its H3(1–15)K4me2-bound counterpart.

Figure 3

a, Intermolecular backbone interactions between the A1–T6 segment of bound H3(1–15)K4me3 peptide and the PHD finger in the complex. b, Intermolecular hydrogen-bonding interactions involving the guanidinium group of R2 in the complex. c, Superposition of free (coloured green) and H3(1–15)K4me3-bound complex (coloured yellow) of the BPTF PHD finger. d, e, Positioning of the trimethylated lysine of the H3(1–15)K4me3 peptide (d) and the dimethylated lysine of the H3(1–15)K4me2 peptide (e) within a four-aromatic-amino-acid cage of the BPTF PHD finger. Two bridging water molecules link the NH of K4me2 to the carboxylate of D6, as indicated by dashed lines.