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- W2090252012 abstract "G-protein coupled receptors catalyze nucleotide exchange on G proteins, which results in subunit dissociation and effector activation. In the recent β 2 AR-G s structure, portions of Switch I and II of Gα are not fully elucidated. We paired fluorescence studies of receptor-Gα i interactions with the β 2 AR-G s and other G i structures to investigate changes in Switch I and II during receptor activation and GTP binding. The β2/β3 loop containing Leu194 of Gα i is located between Switches I and II, in close proximity to IC2 of the receptor and the C-terminus of Gα, thus providing an allosteric connection between these Switches and receptor activation. We compared the environment of residues in myristoylated Gα i proteins in the heterotrimer to that upon receptor activation and subsequent GTP binding. Upon receptor activation, residues in both Switch regions are less solvent-exposed, as compared to the heterotrimer. Upon GTPγS binding, the environment of several residues in Switch I resemble the receptor-bound state, while Switch II residues display effects on their environment which are consistent with their role in GTP binding and Gβγ dissociation. The ability to merge available crystal structures with solution studies is a powerful tool to gain insight into conformational changes associated with receptor-mediated G i protein activation." @default.
- W2090252012 created "2016-06-24" @default.
- W2090252012 creator A5023618339 @default.
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- W2090252012 creator A5068550892 @default.
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- W2090252012 date "2013-10-01" @default.
- W2090252012 modified "2023-10-12" @default.
- W2090252012 title "Linking receptor activation to changes in Sw I and II of Gα proteins" @default.
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- W2090252012 doi "https://doi.org/10.1016/j.jsb.2013.02.016" @default.
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