Article
Role of extracellular disulfide-bonded cysteines in the ligand binding function of the beta 2-adrenergic receptor.
Biochemistry - 6 Mar 1990
Dohlman H G, Caron M G, DeBlasi A, Frielle T, Lefkowitz R J
Abstract excerpt
Evidence is presented for a role of disulfide bridging in forming the ligand binding site of the beta 2-adrenergic receptor (beta AR). The presence of disulfide bonds at the ligand binding site is indicated by "competitive" inhibition by dithiothreitol (DTT) in radioligand binding assays, by specific protection by beta-adrenergic ligands of these effects, and by the requirement of disulfide reduction for limit...
Topics
- Animals
- Binding Sites
- Binding, Competitive
- Cricetinae
- Cysteine
- Disulfides
- Dithiothreitol
- Extracellular Space
- Kinetics
- Ligands
- Mutation
- Receptors, Adrenergic, beta