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. 2019 Apr 2;9:5495. doi: 10.1038/s41598-019-41980-x

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© The Author(s) 2019

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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Rearrangement of contacts in A2aR. (A) Differences between side chain interactions in A2aR and A2aR:Mini-Gs, revealed by analysis of Protein Structure Networks (PSNs). Pink cylinders: predominant contacts in A2aR:Mini-Gs; blue cylinders: predominant contacts in A2aR. The thickness of the cylinders is proportional to the difference in interaction strength. (B) Same analysis for the A2aR:α5 complex. (C) Conformational changes of side chains involved in the redistribution of contacts, that extended from the vicinity of the Mini-Gs binding site to the agonist site. Blue: A2aR; green: A2aR:Mini-Gs. The red arrows indicate the relaxation of W246, F242 and R102 upon removal of Mini-Gs.