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. 2023 Mar 25;14:1659. doi: 10.1038/s41467-023-37259-5

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© The Author(s) 2023

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. 1 — a Chemical structures of the three NAMs. The shared oxindole isostere is labelled red, the variable groups are shown in black. b Cryo-EM map of the GluA1/2_γ8 LBD (Ligand Binding Domain) and TMD (Transmembrane Domain) sectors, associated with LY-481. The colour code of protein, lipid and NAM is indicated below the map. Subunits are also labelled as described in the text (GluA1: A, C; GluA2: B, D; TARP γ8: B’, D’). c Cryo-EM maps of each NAM in side view. TARP γ8 (helix M4) is shown in green, GluA1 (helix M1) in blue. Also shown are three GluA1 residues involved in NAM co-ordination (Tyr519, Met523, Phe527).