Two amino acids within the alpha4 helix of Galphai1 mediate coupling with 5-hydroxytryptamine1B receptors.

@article{Bae1999TwoAA,
  title={Two amino acids within the alpha4 helix of Galphai1 mediate coupling with 5-hydroxytryptamine1B receptors.},
  author={Hyunsu Bae and Theresa M Cabrera-Vera and Karyn M Depree and Stephen G Graber and Heidi E. Hamm},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 21},
  pages={14963-71}
}
We previously reported that residues 299-318 in Galphai1 participate in the selective interaction between Galphai1 and the 5-hydroxytryptamine1B (5-HT1B) receptor (Bae, H., Anderson, K., Flood, L. A., Skiba, N. P., Hamm, H. E., and Graber, S. G. (1997) J. Biol. Chem. 272, 32071-32077). The present study more precisely defines which residues within this domain are critical for 5-HT1B receptor-mediated G protein activation. A series of Galphai1/Galphat chimeras and point mutations were… CONTINUE READING

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