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• W4293661251 abstract "The β 2 adrenergic receptor (β 2 AR), one of important members of the G protein coupled receptors (GPCRs), has been suggested as an important target for cardiac and asthma drugs. Two replicas of Gaussian accelerated molecular dynamics (GaMD) simulations are performed to explore the deactivation mechanism of the active β 2 AR bound by three different substrates, including the agonist (P0G), antagonist (JTZ) and inverse agonist (JRZ). The simulation results indicate that the Gs protein is needed to stabilize the active state of the β 2 AR. Without the Gs protein, the receptor could transit from the active state toward the inactive state. During the transition process, helix TM6 moves toward TM3 and TM5 in geometric space and TM5 shrinks upwards. The intermediate state is captured during the transition process of the active β 2 AR toward the inactive one, moreover the changes in hydrophobic interaction networks between helixes TM3, TM5, and TM6 and the formation of a salt bridge between residues Arg 3.50 and Glu 6.30 drive the transition process. We expect that this finding can provide energetic basis and molecular mechanism for further understanding the function and target roles of the β 2 AR." @default.
• W4293661251 created "2022-08-31" @default.
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• W4293661251 date "2022-08-30" @default.
• W4293661251 modified "2023-09-27" @default.
• W4293661251 title "Exploring the deactivation mechanism of human β2 adrenergic receptor by accelerated molecular dynamic simulations" @default.
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• W4293661251 doi "https://doi.org/10.3389/fmolb.2022.972463" @default.
• W4293661251 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36111136" @default.
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