Identification of residues required for ligand binding to the beta-adrenergic receptor.

摘要: The functional significance of conserved polar amino acids within the putative transmembrane region beta-adrenergic receptor (beta AR) was examined by oligonucleotide-directed mutagenesis hamster gene encoding beta AR and expression mutant genes in COS-7 cells. Although a substitution aspartate at position 113 with an asparagine residue did not affect or processing protein, resulting show detectable binding toward antagonist iodocyanopindolol. Replacement residues positions 79 318, respectively, had no effect on affinity antagonists but reduced agonists 1 order magnitude. Furthermore, we observed that proline 323 serine resulted improper incomplete AR, presumably reflecting role for this folding receptor. Together our previous results from deletion studies, these observations indicate ligand site involves AR.