Structure of two fragments of the third cytoplasmic loop of the rat angiotensin II AT1A receptor. Implications with respect to receptor activation and G-protein selection and coupling.

@article{Franzoni1999StructureOT,
  title={Structure of two fragments of the third cytoplasmic loop of the rat angiotensin II AT1A receptor. Implications with respect to receptor activation and G-protein selection and coupling.},
  author={Lorella Franzoni and Giuseppe Nicastro and Thelma Aguiar Pertinhez and Elsa Oliveira and Cl{\'o}vis Ryuichi Nakaie and A. C. M. Paiva and Shirley Schreier and Alberto Spisni},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 1},
  pages={227-35}
}
The structural bases that render the third intracellular loop (i3) of the rat angiotensin II AT1A receptor one of the cytoplasmic domains responsible for G-protein coupling are still unknown. The three-dimensional structures of two overlapping peptides mapping the entire i3 loop and shown to differently interact with purified G-proteins have been obtained by simulated annealing calculations, using NMR-derived constraints collected in 70% water/30% trifluoroethanol solution. While the NH2… CONTINUE READING

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