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. 2018 Apr 10;9:1372. doi: 10.1038/s41467-018-03314-9

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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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Fig. 7 — Proposed mechanism of allosteric activation of A_2AR by divalent cations. a Using the RTA analysis, regions are colored based on the intensity of degrees of freedom (DOF) transmitted to the G-protein-binding region (depicted in a dashed ellipse) with red regions having highest transmission. b Comparison of intensity of transmission of degrees of freedom to the G-protein-binding site as a result of perturbing rigidity through rigidification of sliding windows of three consecutive windows in the region corresponding to ECL2, with and without cation bridges ascertained by MD simulations. c Cartoon representation for divalent cation bridge of D261-D170 affecting A_2AR activation. d Potential mechanism of disruption of the ionic lock by divalent cation binding