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. 2019 Oct 18;10:2486. doi: 10.3389/fimmu.2019.02486

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Copyright © 2019 Deng, Song, Fujimoto, Piccirillo, Nagai and Greene.

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 model of acetylation at FOXP3 K252 downregulating suppression by destabilizing homodimerization. FOXP3 forms dynamic homodimer via zinc-finger and leucine-zipper domains, which featured as a two-stranded, anti-parallel a-helical coiled-coil. The inter-subunit hydrogen bond formed between Q234 and E248 stabilizes FOXP3 dimer via electrostatic interactions. The Q234-E248 hydrogen bond depends on the unique conformation of the E248 side chain held by K252 residue (left). Acetylation of K252 by p300 neutralizes the positive charges of K252 side chain and decreases its interaction with E248, and as a consequence, breaks the Q234-E248 inter-subunit hydrogen bond. E248-L241 and Q234-M255 form the steric tension to relax and destabilize the FOXP3 homodimerization (right). (Xiaomin Song, Guoping Deng, and Mark I. Greene).