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. 2020 Dec 4;11:6212. doi: 10.1038/s41467-020-20089-0

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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. 3 — a The domain architecture of AIPP3 (lower panel) and the BAH domain construct used for structural and biochemical studies (upper panel). b The immunoblotting results showing the pull-down results for AIPP3-BAH using different histone peptides. The 0.5% inputs serve as positive controls. c The ITC binding curves showing the AIPP3-BAH domain-binding preference for different histone methylation marks (left panel) and different H3K27 methylation levels (right panel). NDB no detectable binding. d The overall structure of the AIPP3-BAH domain H3K27me3 peptide complex shown in ribbon with the AIPP3-BAH domain, and the H3K27me3 peptide colored in green and yellow, respectively. e An electrostatic surface view of AIPP3-BAH domain with the H3K27me3 peptide in the space-filling model showing that the peptide fits inside a negatively charged surface cleft of the AIPP3-BAH domain. f The detailed interaction between AIPP3-BAH domain and the H3K27me3 peptide with the interacting residues highlighted in sticks and the hydrogen bonds highlighted in dashed yellow lines. g, h The ITC binding curves show that the mutations of essential residues for the H3P30 recognition (g) and aromatic cage residues (h) of the AIPP3-BAH domain significantly decrease the binding toward the H3K27me3 peptide. i The ITC binding curves showing the specific preference of the PAIPP2-PHD finger for the unmodified H3K4. j The overall modeled structure of the PAIPP2-PHD finger in complex with the unmodified H3 peptide with the PHD finger and peptide shown in ribbon and space-filling models. The modeled PAIPP2-PHD finger and the modeling template ATXR5 PHD finger are colored in cyan and silver, respectively, and they were superimposed together. k The detailed interaction between the PAIPP2-PHD finger (in cyan) and the unmodified H3K4 peptide with the interacting residues are highlighted in stick model and hydrogen bonds highlighted in dashed yellow lines. The corresponding residues from modeling template ATXR5 (in silver, PDB code: 5VAB) were overlain and highlighted, showing that almost all the interacting residues are conserved. l The ITC binding curves showing that the D306K mutation of PAIPP2-PHD finger, which potentially disrupts H3R2 recognition, totally abolishes the unmodified H3K4 binding by PAIPP2.