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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. 8 — a, Summary graph for time constants of desensitization and recovery from desensitization in outside-out recordings of GluA2 (edited-Gly) with and without TARP γ2. Data are presented as mean ± SD. One-way ANOVA (F_3,54 = 68.40; p < 0.0001)_des; (F_3,65 = 52.99; p < 0.0001)_rec with Sidak’s multiple comparison test (τ_des: TARP-free: p = 0.8849; + γ2: ***p = 0.0001; τ_rec: TARP-free: ****p < 0.0001; + γ2: ****p < 0.0001). Number of patches - τ_des: 11 (wt), 12 (F231A), 20 (wt+ γ2), 15 (F231A + γ2); τ_rec: 22 (wt), 13 (F231A), 18 (wt+ γ2), 16 (F231A + γ2). b, As A, for GluA1/GluA2 (unedited-Arg) heteromers (TARP-free). Data are presented as mean ± SD. Unpaired two-tailed Student’s t-test: t(20) = 2.055; p = 0.0531 (τ_des), t(18) = 2.234; *p = 0.0384 (τ_rec). Number of patches - τ_des: 10 (wt/wt), 12 (wt/F231A); τ_rec: 10 (wt/wt), 10 (wt/F231A). c, The resting state GluA2(F231A)/γ2 LBD-TMD map is shown together with representative 2D class averages, demonstrating the high resolution in the receptor core and the lack of NTD inter-dimer interface. d, Side (left) and top (right) views of representative NTD 3D classes from resting state GluA2(F231A)/γ2 show separation and splaying of the NTD dimers, but less splaying than GluA1/γ3. e, Conformational landscape of resting state GluA2(F231A)/γ2 (pink) and GluA1/γ3 (blue) in the space of splaying angles, with an A2-containing reference structure (PDB: 6QKZ; ‘A2’ red) shown for comparison, shows reduced splaying of GluA2(F231A)/γ2. Representative classes in d are circled with corresponding colors and shown overlaid on the reference structure (right). f, A GluA2(F231A)/γ2 3D NTD class from a non-swapped receptor.

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