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. 2019 Jan 3;10:36. doi: 10.1038/s41467-018-07906-3

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — The ePHD₆ domain of MLL3 specifically binds to the H4H18-containing motif of histone H4. a Superimposition of the structures of the H4 peptide-bound and peptide-free ePHD₆ domain of MLL3. b Cartoon representation of the PHD₆ and preceding zinc finger colored in cyan and purple, respectively. The histone H4 peptide is shown with a Fo–Fc omit map contoured at 2.5 σ. c, e, f Detailed interactions between the ePHD₆ domain of MLL3 and residues A15/K16, R17/R19, and H18 of histone H4 peptide, respectively. The histone H4 peptide is shown in sticks and colored in yellow. Interacting residues are shown in stick mode and red/yellow dashed lines represent intra-molecular hydrogen bonds and atom distances, respectively. d Schematic of the detailed interactions between the ePHD₆ domain of MLL3 and the H4H18 histone H4 peptide. The histone H4 interacting residues of MLL3 are colored in blue. Dashed lines represent hydrogen bonds. g ITC curves for the titration of wild type or different mutants of ePHD₆ domain of MLL3 to the histone H4 peptide H4_11–21. NB no detectable binding, WB, weak binding. h Binding affinities of different histone peptides to ePHD₆ domain of MLL3 and MLL4 measured by ITC