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. 2018 Jul 10;8:10414. doi: 10.1038/s41598-018-28682-6

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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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Structural stabilization promotes mGlu₂ oligomerization. Model for mGlu₂ receptor oligomerization. In the basal state (black arrows), there is a dynamic equilibrium between different conformational states. When a given conformational state of the receptor is stabilized, e.g. by binding of agonist and PAM (active state, green arrows) or antagonist (inactive state, red arrows) it increases the probability that the receptor can interact with other receptors in the same state, given the fact that the interdimeric interfaces are different in the active and the inactive states.