Journal
CELL
Volume 177, Issue 5, Pages 1243-+Publisher
CELL PRESS
DOI: 10.1016/j.cell.2019.04.021
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Funding
- Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Medicine, Tsinghua University
- Deutsche Forschungsgemeinschaft [Sfb740/B6, HI1502/1-2]
- Stiftung Charite
- Einstein Center Digital Future
- NIH [R01GM083118]
- Gauss Center for Supercomputing e.V.
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The crystal structure of the beta 2-adrenergic receptor (beta 2AR) bound to the G protein adenylyl cyclase stimulatory G protein (Gs) captured the complex in a nucleotide-free state (beta 2AR-Gs(empty)). Unfortunately, the beta 2AR-Gs(empty) complex does not provide a clear explanation for G protein coupling specificity. Evidence from several sources suggests the existence of a transient complex between the beta 2AR and GDP-bound Gs protein (beta 2AR-Gs(GDP) ) that may represent an intermediate on the way to the formation of beta 2AR-Gs(empty) and may contribute to coupling specificity. Here we present a structure of the beta 2AR in complex with the carboxyl terminal 14 amino acids from G alpha s along with the structure of the GDP-bound Gs heterotrimer. These structures provide evidence for an alternate interaction between the beta 2AR and Gs that may represent an intermediate that contrib- utes to Gs coupling specificity.
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