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. 2022 Apr 15;36(4):291–311. doi: 10.1007/s10822-022-00452-7

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Molecular structure of a typical bromodomain fold and PHIP2 binding site. The left panel (A) shows the α-helical bundle fold (PDB-ID: 5RJI). The αZ, αA, αB and αC indicate the Z, A, B and C alpha helices, in pink, yellow, cyan and teal, respectively. ZA, AB and BC show the connecting loops of same name, in fuchsia, orange and purple, respectively. The right panel (B) shows the PHIP2 binding site in complex with H4K5acK8ac-like peptide (PDB-ID: 7BBP). The conserved bromodomain 4 water-network is showed in red spheres with the additional PHIP2 water in orange. The atypical threonine 1396 and acetylated lysine (Kac) are displayed in purple and lilac sticks, respectively