期刊
NATURE
卷 558, 期 7711, 页码 553-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41586-018-0215-y
关键词
-
资金
- National Institutes of Health [DK071662]
- American Asthma Foundation
- Jay and Betty Van Andel Foundation
- Ministry of Science and Technology (China) [2012ZX09301001, 2012CB910403, 2013CB910600, XDB08020303, 2013ZX09507001, GM117372, GM0875119]
- Pfizer
- National Natural Science Foundation [31770796]
- Canada Excellence Research Chairs program
- Canadian Institute for Advanced Research
- Anne and Max Tanenbaum Chair in Neuroscience
- Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD
- Frederick National Laboratory for Cancer Research, National Institutes of Health [HHSN261200800001E]
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(s) (stimulatory) and G(i) (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(i) are mediated by the C-terminal helix of the G(i) alpha-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(i)-bound and arrestin-bound forms of rhodopsin with inactive and G(s)-bound forms of the beta(2)-adrenergic receptor provide a foundation to understand the unique structural signatures that are associated with the recognition of G(s), G(i) and arrestin by activated G-protein-coupled receptors.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据