Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function.

@article{Strader1988ConservedAA,
  title={Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function.},
  author={Catherine D. Strader and Irving S. Sigal and Mari Rios Candelore and Elaine Rands and W S Hill and Richard Alastair Dixon},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 21},
  pages={10267-71}
}
Deletion mutagenesis experiments have demonstrated that the binding site of the beta-adrenergic receptor involves the hydrophobic core of the protein (Dixon, R. A. F., Sigal, I. S., Rands, E., Register, R. B., Candelore, M. R., Blake, A. D., and Strader, C. D. (1987) Nature 326, 73-77). Single amino acid replacements for the conserved Asp79 and Asp113 within this putative transmembrane region had profound effects on the ability of the receptor to bind radiolabeled ligands (Strader, C. D., Sigal… CONTINUE READING
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