Abstract
Recent studies on the structure-activity of the kinin B1 receptor (B1R) revealed that important residues for its binding to des-Arg9-bradykinin (DBK) are homologous to those in the interaction between angiotensin II and the angiotensin II (AngII) type I receptor (AT1R). Several studies have shown that the ammonium group of Lys199 (512) located in the helix V of AT1R interacts with the car…