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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. 4 — a, Peaks corresponding to sodium ions observed at the selectivity filter entry in the resting state from top (left) and bottom (right) views. The putative Na⁺ ion is marked with two asterisks. A strong water molecule locates to the periphery of Q583, connecting it with M581 and W602 in a neighboring subunit (this water is denoted with one asterisk). b, side view onto the selectivity filter showing the mobile C585 modelled in double occupancy. c, A putative Na⁺ ion locates to the narrow M3 gate constriction and is coordinated by the four T621 side chains, one from each subunit. d, Open state-specific water molecules that may stabilize the M3 kink, a hallmark of the AMPAR open state. Hydrogen bonds indicated by stippled lines, with distances in Ångstrom shown. All Fo-Fc difference peaks (green mesh) are contoured at 5.5σ. e, Pore dimensions of resting state (stippled lines) and active states (full lines) for GluA1/γ3 (blue) and GluA1/2 (red; PDB: 7OCF). f, Top view of superposed active state GluA1/γ3 and GluA1/2_γ8/CNIH2 (PDB: 7OCF) models, showing close similarity and gating dominance of the B/D chains (black arrows, red glow). g, Top view of superposed GluA1/γ3 models at resting (grey) and open state (colored) shows the asymmetric gate dilation as in B, which is accompanied by widening of the preM1 helices in the active versus resting state.