Structure and conformational changes in the C-terminal domain of the beta2-adrenoceptor: insights from fluorescence resonance energy transfer studies.

@article{Granier2007StructureAC,
  title={Structure and conformational changes in the C-terminal domain of the beta2-adrenoceptor: insights from fluorescence resonance energy transfer studies.},
  author={S. Granier and Samuel C Kim and Aaron M Shafer and Venkata R. P. Ratnala and Juan Jos{\'e} Fung and Richard N. Zare and Brian K. Kobilka},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 18},
  pages={13895-905}
}
The C terminus of the beta(2)-adrenoceptor (AR) interacts with G protein-coupled receptor kinases and arrestins in an agonist-dependent manner, suggesting that conformational changes induced by ligands in the transmembrane domains are transmitted to the C terminus. We used fluorescence resonance energy transfer (FRET) to examine ligand-induced structural changes in the distance between two positions on the beta(2)-AR C terminus and cysteine 265 (Cys-265) at the cytoplasmic end of transmembrane… CONTINUE READING
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