Abstract
The human β1-adrenoceptor (β1AR) is a G-protein-coupled receptor (GPCR) involved in sympathetic system regulation through agonist-induced activation. The conserved CWXP-motif in helix 6 (rotamer toggle switch) is one of the most important activation switches in Class A GPCRs. In order to investigate how the agonist binding disturbs this switch, we carried out molecular dynamics simulations of a hβ1AR model in the apo and R-noradrenaline-bound forms. The results show that the agonist binding changes the β1-angle distribution of Cys336, Trp337 and Phe341 residues and increases the helix 6 bending. Overall, we provide a functional hβ1AR model, showing how the rotamer toggle switch mechanism works at atomic level.
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