Computational Study on the Different Ligands Induced Conformation Change of β2 Adrenergic Receptor-Gs Protein Complex

摘要: β2 adrenergic receptor (β2AR) regulated many key physiological processes by activation of a heterotrimeric GTP binding protein (Gs protein). This process could be modulated different types ligands. But the details about this modulation were still not depicted. Here, we performed molecular dynamics (MD) simulations on structures β2AR-Gs in complex with The simulation results demonstrated that agonist BI-167107 form hydrogen bonds Ser2035.42, Ser2075.46 and Asn2936.55 more than inverse ICI 118,551. modes ligands further affected conformation β2AR. energy landscape profiled contour map stable dissociated Gαs Gβγ when bound to It also showed minimum pathway conformational change along reaction coordinates. By using interactive essential analysis, found domain Gs had tendency separate 118,551 α5-helix relatively quick movement respect transmembrane segments β2AR Besides, analysis centroid distance was separated from during MD simulations. Our only provide induced protein, but supplied information for efficacies drug design