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. 2018 Feb 9;24(10):1489–1501. doi: 10.1038/s41380-017-0011-3

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License, which permits any non-commercial 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. If you remix, transform, or build upon this article or a part thereof, you must distribute your contributions under the same license as the original. 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-nc-sa/4.0/.

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Fig. 3 — Alignment of GluN1-1b receptor amino acid sequence across all mammalian species tested. Regions containing the four peptide sequences (peptides 1–4: P1: AA35–53, P2: AA361–376, P3: AA385–399, and P4: AA660–811) used in the immunization experiment are highlighted in yellow and light brown (compare three-dimensional presentation in Fig. 2c) and nonhomologous amino acids in pink. SP signal peptide, S1, S2 segments of the ligand-binding domain, TMD A transmembrane domain A, TMD B transmembrane domain B, TMD C transmembrane domain C