Abstract：
: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 Gs (stimulatory) and Gi (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 Gi are mediated by the C-terminal helix of the Gi 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, Gi-bound and arrestin-bound forms of rhodopsin with inactive and Gs-bound forms of the β2-adrenergic receptor provide a foundation to understand the unique structural signatures that are associated with the recognition of Gs, Gi and arrestin by activated G-protein-coupled receptors.
journal_name
Naturejournal_title
Natureauthors
Kang Y,Kuybeda O,de Waal PW,Mukherjee S,Van Eps N,Dutka P,Zhou XE,Bartesaghi A,Erramilli S,Morizumi T,Gu X,Yin Y,Liu P,Jiang Y,Meng X,Zhao G,Melcher K,Ernst OP,Kossiakoff AA,Subramaniam S,Xu HEdoi
10.1038/s41586-018-0215-ysubject
Has Abstractpub_date
2018-06-01 00:00:00pages
553-558issue
7711eissn
0028-0836issn
1476-4687pii
10.1038/s41586-018-0215-yjournal_volume
558pub_type
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