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. 2018 Jun 21;9:2425. doi: 10.1038/s41467-018-04836-y

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© The Author(s) 2018

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. 4 — H3K27me3-BAH and H3K4me3-PHD finger binding are independent of each other. a A superposition of PtSHL-H3K27me3 (in colored scheme) and PtSHL-H3K4me3 (in silver) complexes. The distance between H3S10 to H3A21 and the distance between Gly131 and Cys142 as a reference are highlighted as dashed lines. b The ITC binding curve of 2-fold excess H3(20-36)K27me3 pre-saturated PtSHL titrated by H3(1-15)K4me3 peptides. c The ITC binding curve of 2-fold excess H3(1-15)K4me3 pre-saturated PtSHL titrated by H3(20-36)K27me3 peptides. d The binding between PtSHL and H3(1-35)K4me3K27me3 peptide yielded a binding affinity nearly identical as PtSHL-H3K4me3 and PtSHL-H3K27me3 and with an N-value of 1.17