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. 2020 Jul 3;11:3339. doi: 10.1038/s41467-020-17098-4

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© The Author(s) 2020

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 — a A model for the leukemic activity of the NUP98–PHF23 fusion. b Structure of PHF23_PHD. The N-terminus of another PHF23_PHD molecule (white) binds in the histone-binding site of the domain. The side chain of I340 occupies the aromatic cage. Source data are provided in the Source Data file. c, d Identification of the H3K4me3-binding site of PHF23_PHD. Residues that exhibit H3K4me3-induced resonance changes in (d) are mapped onto the structure of PHF23_PHD in (c). Histogram shows NMR chemical shift perturbations in PHF23_PHD upon binding of H3K4me3 peptide at a 1:4 ratio. ‘P’ indicates a proline residue. ‘−’ indicates an unassigned residue. Bars reaching the maximum of y-axis indicate disappeared cross-peaks. Source data are provided in the Source Data file. e Binding affinities of the PHF23_PHD mutants to the H3K4me3 peptide as measured by tryptophan fluorescence (^a) or by NMR titration experiments (^b).