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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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Comparison of the alternative, canonical agonist and antagonist bound structures: (A) Angle displacement between H12 position of alternative ERβ LBD-E2 (red), canonical agonist ERβ LBD-E2 (green, PDB code 3OLS) and antagonist ERβ LBD-genistein (purple, PDB code 1QKM) structures. Alternative structure appears to be in a similar position to the antagonist structure. (B) Distance between the charge-clamp residues (K314 and E493) of alternative ERβ LBD-E2 (H12 in red, residues in cyan) and canonical agonist ERβ LBD-E2 (H12 and residues in green, PDB code 3OLS). The charge clamp of canonical conformation is an optimal distance, since the structure was associated with a coactivator peptide.