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- W1975932489 abstract "The function of G-protein-coupled receptors is tightly modulated by the lipid environment. Long-timescale molecular dynamics simulations (totaling ∼3 μs) of the A2A receptor in cholesterol-free bilayers, with and without the antagonist ZM241385 bound, demonstrate the instability of helix II in the apo receptor in cholesterol-poor membrane regions. We directly observe that the effect of cholesterol binding is to stabilize helix II against a buckling-type deformation, perhaps rationalizing the observation that the A2A receptor couples to G protein only in the presence of cholesterol (Zezula and Freissmuth, 2008Zezula J. Freissmuth M. The A2A adenosine receptor: a GPCR with unique features?.Br. J. Pharmacol. 2008; 153: S184-S190Crossref PubMed Scopus (73) Google Scholar). The results suggest a mechanism by which the A2A receptor may function as a coincidence detector, activating only in the presence of both cholesterol and agonist. We also observed a previously hypothesized conformation of the tryptophan “rotameric switch” on helix VI in which a phenylalanine on helix V positions the tryptophan out of the ligand binding pocket." @default.
- W1975932489 created "2016-06-24" @default.
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- W1975932489 date "2009-12-01" @default.
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- W1975932489 title "A Role for a Specific Cholesterol Interaction in Stabilizing the Apo Configuration of the Human A 2A Adenosine Receptor" @default.
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- W1975932489 doi "https://doi.org/10.1016/j.str.2009.10.010" @default.
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