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. Author manuscript; available in PMC: 2015 Dec 23.
Published in final edited form as: Biochim Biophys Acta. 2014 Apr 18;1839(8):719–727. doi: 10.1016/j.bbagrm.2014.04.011

Fig. 2.

Fig. 2

Structural basis for multivalent readout of multiple histone tails. (A) Ribbon-representation of a model of the BPTF PHD-Bromo cassette simultaneously recognizing H3K4me3 and H4K16ac following superposition of the crystal structures of BPTF PHDBromo-H3(1–15)K4me3 complex (PDB code: 2F6J) and BPTF PHD-Bromo-H4(12–21) K16ac complex (PDB code: 3QZS). The PHD finger, the bromodomain, the linker region and the bound peptides are colored in magenta, green, wheat and yellow, respectively. TheH3K4me3 and H4K16ac are highlighted in stick representations. (B) Ribbon representation of a model of ZMET2 simultaneously recognizing two H3K9me2 peptides with its BAH domain and chromodomain by superposition of the crystal structures of ZMET2-H3(1–15)K9me2 complex (PDB code: 4FT2) and ZMET2-H3(1–32)K9me2 complex (PDB code: 4FT4). The BAH domain, the methyltransferase, the chromodomain and the bound peptides are colored in magenta, wheat, green and yellow, respectively. The two H3K9me2 marks are highlighted in stick representations.