Fig. 1: Cryo-EM structures of A2BR bound to the endogenous ligand ADO and a selective non-nucleoside agonist BAY 60-6583.
From: Structures of adenosine receptor A2BR bound to endogenous and synthetic agonists
a, b Cryo-EM map (a) and structural model (b) of the ADO–A2BR–Gs complex. c, d Cryo-EM map (c) and structural model (d) of the BAY 60-6583–A2BR–Gs protein complex. The ADO (b) and BAY 60-6583 (d) with their density maps are shown. e The sequence alignment of the residues in the ADO-binding pocket among three ARs. f ADO-binding pocket in A2BR. Hydrogen bonds are shown as black dashed lines. g BAY 60-6583-binding pocket in A2BR. h Structure superposition of ADO– and BAY 60-6583–A2BR complexes. Two dashed lines indicate the inserting depth of ADO and BAY 60-6583. i The RMSDs of ADO in A1R, A2AR, and A2BR binding pockets. j Effects of BAY 60-6583 on the wild-type and mutated ARs with the swapped leucine/valine at position 6.51. NanoBiT Assay was performed to evaluate ligand activity in three independent experiments in triplicate (n = 3). k Potential steric hindrance between BAY 60-6583 and L6.51. The mutation was generated by the software PyMOL. l, m Conformational comparison of A2BR and the inactive A2AR (PDB: 4EIY).
