ChEMBL

The latest GPCR structure, published in Nature, adds further to our understanding of the detailed conformational changes that lead to signal transduction for the rhodopsin-like GPCRs - specifically the structure of the active state ternary complex of agonist-activated monomeric β2AR and nucleotide-free Gs heterotrimer. As in most other GPCR structures, engineering of the receptor was performed, and the structure also contains an antibody derived fragment, and an inserted lysozyme domain within the β2AR chain.

Coordinates are accessible at PDBe:3sn6, ligand data is at CHEMBL:1615159

%T Crystal structure of the β2 adrenergic receptor–Gs protein complex
%A S.G.F. Rasmussen
%A B.T. DeVree
%A Y. Zou
%A A.C. Kruse
%A K.Y. Chung
%A T.S. Kobilka
%A F.S. Thian
%A P.S. Chae
%A E. Pardon
%A D. Calinski
%A J.M. Mathiesen
%A S.T.A. Shah
%A J.A. Lyons
%A M. Caffrey
%A S.H. Gellman
%A J. Steyaert
%A G. Skiniotis
%A W.I. Weis
%A R.K. Sunahara
%A B.K. Kobilka
%J Nature 
%D 2011

%V 477

%P 549-555
%O doi:10.1038/nature10361