6EG8

Structure of the GDP-bound Gs heterotrimer

Summary for 6EG8

• Entry DOI: 10.2210/pdb6eg8/pdb
• Descriptor: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, ... (6 entities in total)
• Functional Keywords: g protein heterotrimer gdp gpcr, signaling protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 12
• Total formula weight: 361495.21

Authors

Hilger, D.,Liu, X.,Aschauer, P.,Kobilka, B.K. (deposition date: 2018-08-19, release date: 2019-06-05, Last modification date: 2024-03-13)

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 (2.8 Å)