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• W2926443272 abstract "The alternative inactive state of the human β2-adrenergic receptor originally exposed in molecular dynamics simulations was investigated using various analysis tools to evaluate causality between correlated residue-pair fluctuations and suggest allosteric communication pathways. A major conformational shift observed in the third intracellular loop (ICL3) displayed a novel inactive state, featuring an inaccessible G protein binding site blocked by ICL3 and an expanded orthosteric ligand binding site. Residue-based mean-square fluctuation and stiffness calculations revealed a significant mobility decrease in ICL3, which induced a mobility increase in the remaining loop regions. This indicates conformational entropy loss in one mobile region being compensated by residual intermolecular motions in other mobile regions. Moreover, the extent of significantly correlated motions decreased, and correlations that once existed between transmembrane helices shifted toward regions with increased mobility. Conditional time-delayed cross-correlation analysis identified distinct driver–follower relationship profiles. Prior to its packing, freely moving ICL3 was markedly driven by transmembrane helix-8 whereas once packed, ICL3 controlled future fluctuations of nearby helices. Moreover, two transmembrane helices, (H5 and H6), started to control future fluctuations of a remote site, the extracellular loop, ECL2. This clearly suggests that allosteric coupling between extra- and intracellular parts intensified, in agreement with the receptor’s well recognized feature, which is the inverse proportionality between activity and the degree of coupling." @default.
• W2926443272 created "2019-04-11" @default.
• W2926443272 creator A5001664307 @default.
• W2926443272 creator A5080394142 @default.
• W2926443272 date "2019-04-04" @default.
• W2926443272 modified "2023-10-05" @default.
• W2926443272 title "Intrinsic Dynamics and Causality in Correlated Motions Unraveled in Two Distinct Inactive States of Human β₂-Adrenergic Receptor" @default.
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• W2926443272 doi "https://doi.org/10.1021/acs.jpcb.9b01202" @default.
• W2926443272 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30946584" @default.
• W2926443272 hasPublicationYear "2019" @default.
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