Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6E67

Structure of beta2 adrenergic receptor fused to a Gs peptide

Summary for 6E67
Entry DOI10.2210/pdb6e67/pdb
DescriptorBeta-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 Keywordsg protein coupled receptor, membrane protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight121057.96
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 citationLiu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.7 Å)
Structure validation

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon