Site-directed mutagenesis and continuous expression of human beta-adrenergic receptors. Identification of a conserved aspartate residue involved in agonist binding and receptor activation.

@article{Chung1988SitedirectedMA,
  title={Site-directed mutagenesis and continuous expression of human beta-adrenergic receptors. Identification of a conserved aspartate residue involved in agonist binding and receptor activation.},
  author={F Z Chung and Cheng Dao Wang and Paul Charles Potter and J. C. Venter and Claire M. Fraser},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 9},
  pages={4052-5}
}
Using a new expression vector that allows stable and steroid inducible expression of the human beta 2-adrenergic receptor in mouse L cells, we have examined the functional significance of the highly conserved aspartate residue in the putative second transmembrane region of the receptor. Substitution of aspartate 79 with asparagine produced a mutant receptor that displays the expected affinity and stereoselectivity for antagonists but a 40-, 140-, and 240-fold reduction in its affinity for… CONTINUE READING