4GPO

Oligomeic Turkey Beta1-Adrenergic G Protein-Coupled Receptor

Summary for 4GPO

• Entry DOI: 10.2210/pdb4gpo/pdb
• Descriptor: Beta-1 adrenergic receptor (1 entity in total)
• Functional Keywords: seven-transmembrane helix receptor, g-protein coupled receptor, receptor
• Biological source: Meleagris gallopavo (common turkey,wild turkey)
• Cellular location: Cell membrane; Multi-pass membrane protein: P07700
• Total number of polymer chains: 2
• Total formula weight: 71505.20

Authors

Huang, J.J.,Chen, S.,Zhang, J.J.,Huang, X.Y. (deposition date: 2012-08-21, release date: 2013-02-27, Last modification date: 2024-11-20)

Primary citation

Huang, J.,Chen, S.,Zhang, J.J.,Huang, X.Y.
Crystal structure of oligomeric beta-1-adrenergic G protein-coupled receptors in ligand-free basal state.
Nat.Struct.Mol.Biol., 20:419-425, 2013

PubMed Abstract: G protein-coupled receptors (GPCRs) mediate transmembrane signaling. Before ligand binding, GPCRs exist in a basal state. Crystal structures of several GPCRs bound with antagonists or agonists have been solved. However, the crystal structure of the ligand-free basal state of a GPCR, the starting point of GPCR activation and function, had not yet been determined. Here we report the X-ray crystal structure of the ligand-free basal state of a GPCR in a lipid membrane-like environment. Oligomeric turkey β1-adrenergic receptors display two dimer interfaces. One interface involves the transmembrane domain (TM) 1, TM2, the C-terminal H8 and extracellular loop 1. The other interface engages residues from TM4, TM5, intracellular loop 2 and extracellular loop 2. Structural comparisons show that this ligand-free state is in an inactive conformation. This provides the structural basis of GPCR dimerization and oligomerization.

PubMed: 23435379
DOI: 10.1038/nsmb.2504

Experimental method

X-RAY DIFFRACTION (3.5 Å)