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. 2024 May 22;630(8017):762–768. doi: 10.1038/s41586-024-07475-0

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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 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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Extended Data Fig. 9 — a-d, LBD dimers from structures of GluK2_Glu-asym (a, green), GluA2-GSG1L_Quis (b, PDB ID: 7RYZ, cyan), GluA2-γ5_Quis (c, PDB ID: 7RZ8, olive) and superposition of GluK2_Glu-asym and GluA2-GSG1L_Quis (e) viewed from the side (left) or top (right). The agonist molecules Glu and quisqualate (Quis) are shown as space-filling models. Distances between Cα atoms of S670 and P773 in KARs and S635 and S741 in AMPARs are indicated. Rotation of the lobes D1 towards D2 upon agonist binding is illustrated by blue arrows. Red arrows point to the cleft between the LBD protomers signifying the loss of the dimer 2-fold rotational symmetry.