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. 2017 Jul 10;7:4944. doi: 10.1038/s41598-017-05095-5

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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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(A) 2-Methyl-6-(phenylethynyl)pyridine (MPEP), (B) comparison of MPEP (grey) docking in mGlu5 (light blue), and MPEP (pink) docking in mGlu4 (light green) prior to MD simulations. Selected residues delineating allosteric pockets or participating in ligand binding are labelled (labelling: mGlu5 first, mGlu4 second). Protein-ligand H-bonds are represented by black lines. Helix orientations as follows: TM5 left, TM3 centre-left, TM7 centre-right, TM1 right. TM6 backbone is hidden.