Article
A point mutation in the seventh hydrophobic domain of the alpha 2 adrenergic receptor increases its affinity for a family of beta receptor antagonists.
The Journal of biological chemistry - 15 Aug 1991
Suryanarayana S, Daunt D A, Von Zastrow M, Kobilka B K
Abstract excerpt
Previous studies have shown that differences in subtype-specific ligand binding between alpha 2 and beta 2 adrenergic receptors are largely determined by the seventh hydrophobic domain. Here, we report that a single amino acid substitution (Phe412----Asn) in the seventh hydrophobic domain of the alpha 2 adrenergic receptor reduces affinity for the alpha 2 antagonist yohimbine by 350-fold and increases affinity...
Topics
- Adrenergic beta-Antagonists
- Amino Acid Sequence
- Cell Line
- Dihydroalprenolol
- Fluorescent Antibody Technique
- Humans
- Molecular Sequence Data
- Mutation
- Oxygen
- Pindolol
- Receptors, Adrenergic, alpha