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. 2017 Jul 31;7:6933. doi: 10.1038/s41598-017-07292-8

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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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UBP684 potentiation is dependent on GluN2 LBD flexibility. (A) Current traces showing the effect of UBP684 on wildtype, GluN1 LBD-locked (GluN1^C/GluN2^WT) or GluN2 LBD-locked (GluN1^WT/GluN2^C) receptors. (B) UBP684 potentiated wildtype and GluN1 LBD-locked receptors but not GluN2 LBD-locked receptors (one-way ANOVA followed by Tukey’s test; P = 0.0012 and 0.0093 for GluN1^WT/GluN2A^c compared to GluN1^WT/GluN2A^WT and GluN1^C/GluN2A^WT respectively; N = 19–32). (C) Molecular modeling of UBP684 binding to the GluN1/GluN2A receptor LBD dimer. Top: UBP684 (space filled) is shown docked into the GluN1/GluN2A LBD intersubunit interface. Modeling suggests that the carboxylic acid group of UBP684 interacts with positively charged residues on the top of the LBD away from the transmembrane domains and near the N-terminal domains. The alkyl side chain terminates near the LBD hinge region near GluN1 Y535 shown in green. Bottom: The same docking of UBP684 is shown rotated 90° in the horizontal plane with the GluN1 LBD removed and GluN1’s Y535 shown for reference.