Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling.

@article{Moro1993HydrophobicAA,
  title={Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling.},
  author={Osvaldo Moro and Jelveh Lameh and Petra H{\"o}gger and Wolfgang Sadee},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 30},
  pages={
          22273-6
        }
}
Signal transduction of the heptahelical G protein-coupled receptors (GPCRs) involves multiple receptor domains, but a universal consensus domain for coupling has not yet been defined. Alanine mutagenesis scanning was performed on the intracellular loops and the COOH tail of the human muscarinic cholinergic receptor (Hm1) to identify coupling domains. Stimulation of phosphatidylinositol (PI) turnover was determined after transfection of the alanine mutants into U293 human embryonic kidney cells… CONTINUE READING

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