Conformational changes in the G protein Gs induced by the β2 adrenergic receptor

Ka Young Chung, Søren G. F. Rasmussen, Tong Liu, Sheng Li, Brian T. DeVree, Pil Seok Chae, Diane Calinski, Brian K. Kobilka (), Virgil L. Woods () and Roger K. Sunahara ()
Additional contact information
Ka Young Chung: Stanford University School of Medicine
Søren G. F. Rasmussen: Stanford University School of Medicine
Tong Liu: Biomedical Sciences Graduate Program and UCSD DXMS Proteomics Resource, University of California San Diego
Sheng Li: Biomedical Sciences Graduate Program and UCSD DXMS Proteomics Resource, University of California San Diego
Brian T. DeVree: University of Michigan Medical School
Pil Seok Chae: University of Wisconsin
Diane Calinski: University of Michigan Medical School
Brian K. Kobilka: Stanford University School of Medicine
Virgil L. Woods: Biomedical Sciences Graduate Program and UCSD DXMS Proteomics Resource, University of California San Diego
Roger K. Sunahara: University of Michigan Medical School

Nature, 2011, vol. 477, issue 7366, 611-615

Abstract: X-ray structure of a GPCR complex G-protein-coupled receptors (GPCRs) mediate the majority of a cell's responses to hormones and neurotransmitters, and to the senses of sight, olfaction and taste. This makes GPCRs potentially the most important group of drug targets in the human body. GPCRs are deeply embedded in the cell membrane, crossing it seven times, so structure determination for these complexes is particularly challenging — as recounted in a recent News Feature (see http://go.nature.com/ftqnx4 ). The eagerly-awaited X-ray crystal structure of a GPCR transmembrane signalling complex has now been determined by Brian Kobilka's group. The structure presented is of an agonist-occupied monomer of the β2 adrenergic receptor in complex with Gs, the stimulatory G protein for adenylyl cyclase. An accompanying paper reports the use of peptide amide hydrogen-deuterium exchange mass spectrometry to probe the protein dynamics of this signalling complex.

Date: 2011
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DOI: 10.1038/nature10488

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