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. 2018 Jun 25;8:9631. doi: 10.1038/s41598-018-27790-7

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© The Author(s) 2018

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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Concentration-response curves of TAAR13c mutants. HEK293T cells were stably transfected with TAAR13c constructs either altered by single or double point mutations. A cell line expressing TAAR13c wildtype receptors was included for control. Cadaverine and putrescine were added in the range of 0.1 µM to 1 mM. The resulting calcium increase was detected by Fluo-4 and calculated as ∆F/F and normalized to the value obtained with 10 µM NKH477, an agonist of membrane-bound adenylyl cyclases. Left column, response to cadaverine; right column, response to putrescine. Representative binding curves shown for the wildtype receptor and mutants (TAAR13c wildtype, black; D279R, red; D112E/D279N, green). Right panel, insets show mutant side chains (D279N, pale brown; D279R, pink; D112E, blue) overlaying the wildtype residue D in grey. (a) The cadaverine affinity of the D279R mutant was approximately 5fold higher compared to wildtype. (b) The double mutant D112E/D279N had a similar cadaverine affinity as the wildtype receptor with a slight increase in efficacy. For putrescine the affinities of mutant and wildtype TAAR13c receptors were also similar.