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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. 3 — a Model of the receptor complex with JNJ-059 (yellow spheres), highlighting the proximity between the NAM pocket and the GluA1 pre-M1 helix (the figure is derived from an MD simulation). b JNJ-059 disrupts Tyr519 interaction with Tyr206 (γ8) (top panel), as compared to a simulation without the NAM (‘Apo’; bottom panel), but enables an H-bond between Tyr519 and Asp515 in the pre-M1 helix (top). c Variations in distance between centres of mass for Tyr519-Asp515 and Tyr519-Tyr206 in MD simulations of resting-state models. Distances are compared for the apo state (grey) and the JNJ059-bound structure (blue). Data are for both GluA1 subunits (chains A and C) shown in light and dark colours. d Cryo-EM map of the resting-state JNJ-059 structure. Lipid densities stacking along the GluA1 pre-M1 helix are shown in shades of blue (L1-3). e, f Overlay between the JNJ-059-resting model (coloured) with an apo resting state (PDB: 7OCD; grey). e The NAM induces an interaction between Met523 and the acyl chain of lipid L1 (side view, left; top view right), and a rearrangement of L2 via the Tyr519 side chain (f). NAM-induced side chain reorientations are highlighted with an asterisk. The flurophenyl group interacting with L1 is denoted ‘FP’. Note the dilation of the NAM pocket in the presence of JNJ-059.