Abstract:
:The crystal structure of the β2-adrenergic receptor (β2AR) bound to the G protein adenylyl cyclase stimulatory G protein (Gs) captured the complex in a nucleotide-free state (β2AR-Gsempty). Unfortunately, the β2AR-Gsempty 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 β2AR and GDP-bound Gs protein (β2AR-GsGDP) that may represent an intermediate on the way to the formation of β2AR-Gsempty and may contribute to coupling specificity. Here we present a structure of the β2AR in complex with the carboxyl terminal 14 amino acids from Gαs along with the structure of the GDP-bound Gs heterotrimer. These structures provide evidence for an alternate interaction between the β2AR and Gs that may represent an intermediate that contributes to Gs coupling specificity.
journal_name
Celljournal_title
Cellauthors
Liu X,Xu X,Hilger D,Aschauer P,Tiemann JKS,Du Y,Liu H,Hirata K,Sun X,Guixà-González R,Mathiesen JM,Hildebrand PW,Kobilka BKdoi
10.1016/j.cell.2019.04.021subject
Has Abstractpub_date
2019-05-16 00:00:00pages
1243-1251.e12issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(19)30440-4journal_volume
177pub_type
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