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. 2019 Jul 2;10:2915. doi: 10.1038/s41467-019-10853-2

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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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Fig. 6 — NMR study on the interaction of α12 with the FXR-LBD core domain. a Model depicting transient interaction of the AF2 helix with the core domain. b Superimposition of ¹H, ¹⁵N-HSQC of fully 13C/15N-labeled FXR-LBD (blue) and an AF2 truncated FXR-LBD mutant (red) reveals significant shifts and disappearance of signals indicating that α12 interacts transiently with the core domain of the FXR-LBD even in the absence of a ligand/agonist