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. 2024 Jan 2;15:108. doi: 10.1038/s41467-023-44601-4

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© The Author(s) 2024

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. 3 — A Sequence alignment of residues in conserved positions within the OBP of TA1 (top), with highlighted differences between hTA1 and rTA1 (red) or mTA1 (green). Locations of differences with rTA1 (red) or mTA1 (green) are further highlighted on the structure of hTA1. Different residues in the OBP of hTA1, rTA1, and mTA1 are shown in cyan. D^3.32 is highlighted for spatial reference and Ro5256390 is shown in magenta. B Effects of species-related mutations in the OBP on the potency and efficacy hTA1 agonists. Data are expressed as differences between mutant and wild type receptor with potencies determined as pEC₅₀s and efficacies measured as E_max. Data represent mean of two (n = 2; I290^7.39N, V184^EL2P) or three (n = 3; I290^7.39Y, T194^5.42A) independent experiments. See Supplementary Table 1 for fitted parameter values.