Article
Mutation of an aspartate at residue 89 in somatostatin receptor subtype 2 prevents Na+ regulation of agonist binding but does not alter receptor-G protein association.
Molecular pharmacology - 1 Aug 1993
Kong H, Raynor K, Yasuda K, Bell G I, Reisine T
Abstract excerpt
Sodium ions have been shown to reduce the binding of agonists to a number of G protein-linked receptors. They are believed to do so by interacting with aspartate residues in the second membrane-spanning region of these receptors to cause G protein uncoupling, resulting in a diminished affinity of...
Topics
- Animals
- Aspartic Acid
- Base Sequence
- Binding Sites
- CHO Cells
- Cricetinae
- Cricetulus
- GTP-Binding Proteins
- Guanosine 5'-O-(3-Thiotriphosphate)
- Mice
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Peptides, Cyclic
- Pertussis Toxin
- Receptors, Somatostatin
- Sodium
- Somatostatin