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Kang, Yanyong; Kuybeda, Oleg; de Waal, Parker W; Mukherjee, Somnath; Van Eps, Ned; Dutka, Przemyslaw; Zhou, X Edward; Bartesaghi, Alberto; Erramilli, Satchal; Morizumi, Takefumi; Gu, Xin; Yin, Yanting; Liu, Ping; Jiang, Yi; Meng, Xing; Zhao, Gongpu; Melcher, Karsten; Ernst, Oliver P; Kossiakoff, Anthony A; Subramaniam, Sriram; Xu, H Eric
Nature (London), 06/2018, Letnik: 558, Številka: 7711Journal Article
G-protein-coupled receptors comprise the largest family of mammalian transmembrane receptors. They mediate numerous cellular pathways by coupling with downstream signalling transducers, including the hetrotrimeric G proteins G (stimulatory) and G (inhibitory) and several arrestin proteins. The structural mechanisms that define how G-protein-coupled receptors selectively couple to a specific type of G protein or arrestin remain unknown. Here, using cryo-electron microscopy, we show that the major interactions between activated rhodopsin and G are mediated by the C-terminal helix of the G α-subunit, which is wedged into the cytoplasmic cavity of the transmembrane helix bundle and directly contacts the amino terminus of helix 8 of rhodopsin. Structural comparisons of inactive, G -bound and arrestin-bound forms of rhodopsin with inactive and G -bound forms of the β -adrenergic receptor provide a foundation to understand the unique structural signatures that are associated with the recognition of G , G and arrestin by activated G-protein-coupled receptors.
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