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. 2022 Feb 17;12:2691. doi: 10.1038/s41598-022-06591-z

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Homology modeling of TAAR9 predicts the intra-receptor interactions. (a) Homology modeling of mTAAR9 shows typical 7 transmembrane domains (colored according to residue position). Left: Side view. Right: Extracellular view. (b) Detailed inter-helical non-covalent interactions in TAAR9 from extracellular side view. Residue numbers were assigned following numbering scheme in GPCRdb¹². Dotted lines represent presence of inter-helical interactions. Those interactions are mainly composed of hydrogen bonds (deep yellow) and aromatic-hydrogen bonds (cyan), with a few salt bridges (magenta) and pi-pi interactions (blue). An overview of inter-helical interactions network is shown in upper right, with thicker lines indicating stronger interactions. (c) Interactions between TM and N-terminal, TM and ECL, inter-ECL. Besides those interactions described in between TMs, disulfide bond (black lines) is observed between C190^45.50 and C105^3.25. Only residues in TM1, 2, 3, 5, 6 show interaction with extracellular domains.