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. 2019 Jan 24;9:439. doi: 10.1038/s41598-018-36881-4

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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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Proposed complex formation of the promiscuous arrestin-1 quadruple mutant with P-ROS and ROS* in comparison to the arrestin-1 WT bound P-ROS*. WT arrestin-1 has been shown to need both, electrostatic interactions via the GPCR C-terminal tail, as well as the conformational docking with the GPCR cytoplasmic cavity to form a stable interaction with rhodopsin. The shown data suggest that the arrestin-1 (R171A, T304A, E341A, F375A) quadruple mutant is additionally able to utilize both interactions individually to form a stable rhodopsin–arrestin-1 complex.