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. Author manuscript; available in PMC: 2018 Oct 3.
Published in final edited form as: Structure. 2017 Sep 14;25(10):1530–1539.e3. doi: 10.1016/j.str.2017.08.009

Figure 5. pH-sensitivity is conserved in DIDO-PHD but not in Bye1-PHD.

Figure 5

(a) Alignment of amino acid sequences of the PHD fingers: absolutely, moderately and weakly conserved residues are colored orange, pale yellow, and light green, respectively. The aromatic cage residues of the PHD fingers, for which the atomic-resolution structures of the complexes with H3K4me3 have been determined, are indicated by red ovals. (b–d) Structural overlays of the H3K4me3-bound PHD fingers of PPS (this work) and DIDO (PDB 4L7X), PHF13 (PDB 3O7A), and MLL1 (PDB 3LQJ). (e, i) Representative binding curves used to determine the Kds for DIDO and Bye1. (f, h) Binding affinities of DIDO-PHD and Bye1-PHD to H3K4me3 peptide at indicated pH. (g) A model of the Bye1-PHD finger fold generated with Phyre2.