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. 2020 Aug 14;3:446. doi: 10.1038/s42003-020-01160-4

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© The Author(s) 2020

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. 4 — a–g Molecule A (green) in the closed form. h–l Molecule C (salmon) in the open form. In the closed form, Arg267 (the NT region of helix V) hydrogen bonds with Tyr209 (helix III) and Tyr317 (helix VI) as viewed from the intracellular side (a), thereby constricting the major cavity (b). Pro261 (ICL2) and Arg264 (NT) interact with Lys105 and/or Asp106 of NGD (c), Arg264 and Gln265 (NT) interact with Tyr317, Ala318, and Arg320 (helix VI) (d), and Gln254 (helix IV) and Asp256 (ICL2) interact with Lys206 (helix III) (e) in the closed form. In contrast, in the open form, these interactions are completely disrupted (j–l). In both forms, Arg257 and Thr260 interact with His263 within ICL2 (f, h) and Phe258 (ICL2) interacts with Val252 (helix IV) and Thr266 (helix V) (g, i).