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. 2017 Jun 14;7:3509. doi: 10.1038/s41598-017-03774-x

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© The Author(s) 2017

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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Stability of H12 canonical position in ER subtypes: (A) Comparison of main interactions between H12 and the remaining canonical LBD structures of the ERα LBD-E2 (blue, PDB code 1QKU) and ERβ LBD-E2 (green, PDB code 3OLS). ERα LBD-E2 has three hydrophilic interactions stabilizing H12 in its canonical position while ERβ LBD-E2 has only one interaction. The position of histidine H498 was not obtained in 3OLS structure. Its position was added based on the structure of the phosphorylated ERβ LBD-E2 (PDB code 3OLL). (B) RMSD distribution of H12 computed with respect to MD simulation average structures of wild-type ERα LBD-E2 (blue), wild-type ERβ LBD-E2 (green) and K300N mutant of ERβ LBD-E2 (K300Nβ). H12 of wild-type ERα shows a lower mobility than wild-type ERβ. K300Nβ corresponds to the transformation β → α of one of the residues that stabilizes H12. As expected, this mutation reduces the mobility of this helix.