Ligand binding to the beta-adrenergic receptor involves its rhodopsin-like core

Nature. 1987 Mar 5-11;326(6108):73-7. doi: 10.1038/326073a0.


Recently the genes for several hormone receptors that interact with guanine nucleotide binding proteins (G proteins) have been cloned, including the hamster beta 2-adrenergic receptor (beta 2AR), a human beta AR, the turkey erythrocyte beta AR and the porcine muscarinic acetylcholine receptor (MAR). All these receptors share some amino-acid homology with rhodopsin, particularly in 7 hydrophobic stretches of residues that are believed to represent transmembrane helices. To determine whether differences in ligand specificity result from the divergence in the sequences of the hydrophilic regions of these receptors, we have expressed in mammalian cells genes for the wild-type hamster and human beta AR proteins, and a series of deletion mutant genes of the hamster beta 2AR. The pharmacology of the expressed receptors indicates that most of the hydrophilic residues are not directly involved in the binding of agonists or antagonists to the receptor. In addition, we have identified a mutant receptor that has high agonist affinity but does not couple to adenylate cyclase.

MeSH terms

  • Adenylyl Cyclases / metabolism
  • Adrenergic beta-Agonists / metabolism*
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cell Membrane / metabolism
  • Cricetinae
  • Epinephrine / metabolism
  • Humans
  • Iodocyanopindolol
  • Isoproterenol / metabolism*
  • Mutation
  • Norepinephrine / metabolism
  • Pindolol / analogs & derivatives*
  • Pindolol / metabolism
  • Receptors, Adrenergic, beta / genetics
  • Receptors, Adrenergic, beta / metabolism*
  • Rhodopsin
  • Transfection


  • Adrenergic beta-Agonists
  • Receptors, Adrenergic, beta
  • Iodocyanopindolol
  • Rhodopsin
  • Pindolol
  • Adenylyl Cyclases
  • Isoproterenol
  • Norepinephrine
  • Epinephrine