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. 2023 Sep 13;621(7980):877–882. doi: 10.1038/s41586-023-06528-0

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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 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. 7 — a, Side view of cryo-EM density and model of GluA1/γ3 LBD dimer in resting and active states. b, Top of resting GluA1/γ3 LBD dimer interfaces aligned to those from a GluA1/2 heteromer (PDB: 7OCD), showing close similarity despite the presence of the R739 bridge. c, A zoomed view into the arginine bridge between R739 residues resulting from lack of an R/G editing site in active GluA1 supported by strong density shown for the open state as seen for R/G-unedited GluA2 LBD (PDB: 2UXA). A similar arrangement is also seen in the resting state (not shown). d, Electrostatic maps from APBS showing the dispersal of positive charge around R739 in GluA1 compared to the GluA1/2 heteromer, contoured from −10kT/e (red) to + 10kT/e (blue).