Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations.

@article{Dror2009IdentificationOT,
  title={Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations.},
  author={Ron O. Dror and Daniel H. Arlow and David W. Borhani and Morten \O. Jensen and Stefano Piana and David E. Shaw},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 12},
  pages={4689-94}
}
Fully understanding the mechanisms of signaling proteins such as G protein-coupled receptors (GPCRs) will require the characterization of their conformational states and the pathways connecting those states. The recent crystal structures of the beta(2)- and beta(1)-adrenergic receptors in a nominally inactive state constituted a major advance toward this goal, but also raised new questions. Although earlier biochemical observations had suggested that these receptors possessed a set of contacts… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 70 extracted citations

Membrane Organization and Dynamics

Springer Series in Biophysics • 2017

References

Publications referenced by this paper.
Showing 1-10 of 50 references

Structure of a 1-adrenergic G-protein-coupled receptor

T Warne
Nature • 2008
View 6 Excerpts
Highly Influenced

Activation of the 2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6

JA Ballesteros
J Biol Chem • 2001
View 7 Excerpts
Highly Influenced

Crystal structure of opsin in its G-protein-interacting conformation

P Scheerer
Nature • 2008
View 3 Excerpts
Highly Influenced

Functional role of the ‘‘ionic lock’’—an interhelical hydrogen bond network in family A heptahelical receptors

R Vogel
J Mol Biol • 2008

Similar Papers

Loading similar papers…