Fig. 3.

DN13 interacts at the lobe 2 crevice on the activated mGlu2 VFT dimer. a, b View of the proposed docking of DN13 (orange) on the mGlu2 extracellular domain dimer (a, lateral view, b, top view). c Detailed view of the proposed docking of DN13 illustrating proposed residues involved in selectivity, shown are Leu226 and Arg445 in protomer A, and Ser246, Ala248 (yellow), Ala249, and Glu251 in protomer B. d Saturation binding curves of DN13 on mGlu2 WT, mGlu2 bearing mGlu3 specific residues from protomer A (mut A), mGlu2 bearing mGlu3 residues from protomer B (mut B), mGlu2 A248K mutant. e Saturation binding curves of DN13 on mGlu3 WT, mGlu3 bearing the mGlu2 residues on protomer A (mut A), and mGlu3 bearing all identified residues of mGlu2 (mut AB) in cells co-transfected with EAAC1. Data are mean ± SD of triplicates from a typical experiment representative of three experiments