6E67

Structure of beta2 adrenergic receptor fused to a Gs peptide

Summary for 6E67

• Entry DOI: 10.2210/pdb6e67/pdb
• Descriptor: Beta-2 adrenergic receptor,Endolysin,Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,Beta-2 adrenergic receptor chimera, 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydroxy-2H-1,4-benzoxazin-3(4H)-one (2 entities in total)
• Functional Keywords: g protein coupled receptor, membrane protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 121057.96

Authors

Liu, X.,Xu, X.,Hilger, D.,Tiemann, J.,Liu, H.,Du, Y.,Hirata, K.,Sun, X.,Guixa-Gonzalez, R.,Mathiesen, J.,Hildebrand, P.,Kobilka, B. (deposition date: 2018-07-24, release date: 2019-06-05, Last modification date: 2024-11-20)

Primary citation

Liu, X.,Xu, X.,Hilger, D.,Aschauer, P.,Tiemann, J.K.S.,Du, Y.,Liu, H.,Hirata, K.,Sun, X.,Guixa-Gonzalez, R.,Mathiesen, J.M.,Hildebrand, P.W.,Kobilka, B.K.
Structural Insights into the Process of GPCR-G Protein Complex Formation.
Cell, 177:1243-1251.e12, 2019

PubMed 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-Gs). Unfortunately, the β2AR-Gs 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-Gs) that may represent an intermediate on the way to the formation of β2AR-Gs 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.

PubMed: 31080070
DOI: 10.1016/j.cell.2019.04.021

Experimental method

X-RAY DIFFRACTION (3.7 Å)