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- W2950967599 abstract "Membranes are known to have modulatory effects on G protein-coupled receptors (GPCRs) via specific lipid interactions. However, the mechanisms of such modulations in physiological conditions and how they influence GPCR functions remain unclear. Here we report coarse-grained molecular dynamics simulations on the Adenosine A2a receptor in different conformational states embedded in an in vivo-mimetic membrane model. Nine lipid interaction sites were revealed. The strength of lipid interactions with these sites showed a degree of dependence on the conformational states of the receptor, suggesting that these lipids may regulate the conformational dynamics of the receptor. In particular, we revealed a dual role of PIP2 on A2aR activation that involves both stabilization of the characteristic outward tilt of TM6 and enhancement of A2aR-mini-Gs association. Our results demonstrated that the bound lipids allosterically regulate the functional properties of GPCRs. These protein-lipid interactions provide a springboard for design of allosteric modulators of GPCRs." @default.
- W2950967599 created "2019-06-27" @default.
- W2950967599 creator A5003402066 @default.
- W2950967599 creator A5017053527 @default.
- W2950967599 creator A5042299875 @default.
- W2950967599 creator A5068989186 @default.
- W2950967599 date "2019-02-01" @default.
- W2950967599 modified "2023-10-16" @default.
- W2950967599 title "State-dependent Lipid Interactions with the A2a Receptor Revealed by MD Simulations Using In Vivo-Mimetic Membranes" @default.
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- W2950967599 doi "https://doi.org/10.1016/j.str.2018.10.024" @default.
- W2950967599 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7031699" @default.
- W2950967599 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30581046" @default.
- W2950967599 hasPublicationYear "2019" @default.