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. 2019 Apr 1;9:5441. doi: 10.1038/s41598-019-41819-5

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© The Author(s) 2019

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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Evolutionary and structural context of H59 in the DNA–binding domain of human FoxP1. (a) Sequence alignment of the DNA–binding domain from representative members of the human Fox subfamilies. Histidines highlighted in yellow and blue are the family–conserved and the M/O/P subfamily-specific residues, respectively. A secondary structure topology scheme is shown at the bottom of the sequence alignment. (b) Cartoon representation of the structure of the A39P/C61Y monomeric mutant (PDB 2KIU) and the domain–swapped dimer (generated by homology modelling using FoxP2 as template) of the forkhead domain of human FoxP1, showing the position of the two histidine residues (H54 and H59) as sticks. Hydrophobic residues surrounding H54 and H59 at 5 Å are shown in grey using their van der Waals radius.