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. 2022 Aug 10;12:906807. doi: 10.3389/fonc.2022.906807

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Copyright © 2022 Yu, Jia, Ma, Ji, Wang, Liang, Zhang, Yi and Zeng

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Structure of ASH1L PHD finger binding with the H3 (1–15) K4me2 peptide. (A) Cartoon representation of the NMR structure of the ASH1L PHD finger (light blue)/H3K4me2 peptide (yellow). (B) Electrostatic potential surface representation of the ASH1L PHD finger binding with H3K4me2 peptide in stick depiction (color-coded by atom type). The amino acid around the K4 residue and in the β2 strand are labeled. (C) The key residues involved in the intermolecular interactions at the protein/peptide interface are labeled. These side chains are color-coded by the atom type and showed in the stick model. (D) The key side chains of binding groove around K4me2 are picked out.