Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor.

@article{Perlman1997InteractionsBC,
  title={Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor.},
  author={Jeffery H Perlman and Anny Colson and Wenning Wang and Kendra Bence and R. Ben Osman and Marvin C Gershengorn},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 18},
  pages={11937-42}
}
The roles of conserved residues in transmembrane helices (TMs) of G protein-coupled receptors have not been well established. A computer-generated model of the thyrotropin-releasing hormone receptor (TRH-R) indicated that conserved Asp-71 (TM-2) could interact with conserved asparagines 316 (TM-7) and 43 (TM-1). To test this model, we constructed mutant TRH-Rs containing polar or alanine substitutions of these residues. The maximal activities of N43A and N316A TRH-Rs were diminished, whereas… CONTINUE READING
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