Substitution of lysine-181 to aspartic acid in the third transmembrane region of the endothelin (ET) type B receptor selectively reduces its high-affinity binding with ET-3 peptide.

Abstract excerpt

In the G protein-coupled receptor family, a highly conserved aspartic acid located within the third transmembrane domain has been shown to be involved in ligand binding. Within the endothelin (ET) peptide receptor family, this aspartic acid has been replaced by a lysine. To assess the importance...

Topics

• Animals
• Aspartic Acid
• Binding Sites
• Cell Line
• Endothelins
• GTP-Binding Proteins
• Lysine
• Mutation
• Phosphatidylinositols
• Polymerase Chain Reaction
• Radioligand Assay
• Rats