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. 2018 Sep 14;9:3748. doi: 10.1038/s41467-018-06145-w

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© The Author(s) 2018

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. 7 — MD simulations show that constraining the conserved glycine in GluN1 prevents C-terminal expansion of the M4 as observed in wild type. a Cα RMSDs of the ion channel cores (M1–M3, thick lines) and M4s (thin lines) as a function of simulation time for open state models: wild-type GluN1/GluN2B, light orange; GluN1(G815A)/GluN2B, light blue; GluN1/GluN2B(G820A), maroon (see Methods). b Average RMSD values (250–500 ns). Error bars are standard deviations. c, d Open state of wild-type GluN1/GluN2B TMD shown either top down (c) or side views (d) of the GluN1 (left) or GluN2B (right) M4s. All displayed structures are snapshots close to the average structures calculated over 250–500 ns. e, f GluN1(G815A) overlaid on wild type either from top down (e) or with a side view (f). g Displacements between GluN1(G815A) and wild type for M4 residues in the A and C subunits. h, i GluN2B(G820A) overlaid on wild type either from top down (h) or with a side view (i). j Displacements between GluN2B(G820A) and wild type for M4 residues in the B and D subunits