Structural highlights
Function
[ADRB2_HUMAN] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
Publication Abstract from PubMed
The crystal structure of the beta2-adrenergic receptor (beta2AR) bound to the G protein adenylyl cyclase stimulatory G protein (Gs) captured the complex in a nucleotide-free state (beta2AR-Gs(empty)). Unfortunately, the beta2AR-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 beta2AR and GDP-bound Gs protein (beta2AR-Gs(GDP)) that may represent an intermediate on the way to the formation of beta2AR-Gs(empty) and may contribute to coupling specificity. Here we present a structure of the beta2AR in complex with the carboxyl terminal 14 amino acids from Galphas along with the structure of the GDP-bound Gs heterotrimer. These structures provide evidence for an alternate interaction between the beta2AR and Gs that may represent an intermediate that contributes to Gs coupling specificity.
Structural Insights into the Process of GPCR-G Protein Complex Formation.,Liu X, Xu X, Hilger D, Aschauer P, Tiemann JKS, Du Y, Liu H, Hirata K, Sun X, Guixa-Gonzalez R, Mathiesen JM, Hildebrand PW, Kobilka BK Cell. 2019 May 16;177(5):1243-1251.e12. doi: 10.1016/j.cell.2019.04.021. Epub, 2019 May 9. PMID:31080070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu X, Xu X, Hilger D, Aschauer P, Tiemann JKS, Du Y, Liu H, Hirata K, Sun X, Guixa-Gonzalez R, Mathiesen JM, Hildebrand PW, Kobilka BK. Structural Insights into the Process of GPCR-G Protein Complex Formation. Cell. 2019 May 16;177(5):1243-1251.e12. doi: 10.1016/j.cell.2019.04.021. Epub, 2019 May 9. PMID:31080070 doi:http://dx.doi.org/10.1016/j.cell.2019.04.021
