Naturally evolved G protein-coupled receptors adopt metastable conformations.

@article{Chen2012NaturallyEG,
  title={Naturally evolved G protein-coupled receptors adopt metastable conformations.},
  author={Kuang-Yui M. Chen and Fuguo Zhou and Bartlomiej G Fryszczyn and Patrick Barth},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2012},
  volume={109 33},
  pages={
          13284-9
        }
}
A wide range of membrane receptors signal through conformational changes, and the resulting protein conformational flexibility often hinders their structural studies. Because the determinants of membrane receptor conformational stability are still poorly understood, identifying a minimal set of perturbations stabilizing a membrane protein in a given conformation remains a major challenge in membrane protein structure determination. We present a novel approach integrating bioinformatics… CONTINUE READING

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References

Publications referenced by this paper.
SHOWING 1-10 OF 52 REFERENCES

Conformational thermostabilization of the beta1-adrenergic receptor in a detergent-resistant form.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2008
VIEW 4 EXCERPTS
HIGHLY INFLUENTIAL

Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist

K Haga
  • Nature
  • 2012

Computational design of membrane proteins.

  • Current opinion in structural biology
  • 2011