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. 2017 Apr 21;7:1050. doi: 10.1038/s41598-017-01146-z

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© The Author(s) 2017

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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MD simulated ion channel open state. (A,B) MD simulated structure of GluA2 ion channel in the open state (see Methods and text) viewed extracellularly (A) or parallel to the membrane (B). The pore axis is illustrated by a black arrow. (C) Closed channel from GluA2_apo structure (PDB ID: 5L1B) viewed extracellularly. (D) Superposition of the ion channel open (purple) and closed (green) conformations from (A and B) respectively. Blue ovals designate the noncompetitive inhibitor binding pockets.