Fig. 4
a–a′ Prediction of the functional effect of p.Gly471Arg variant by Mutation Taster. b–b′ Differences in hydrogen bond connections between wild-type and mutated models: Gly471 establishes three hydrogen bonds with Arg197 and Asn468 (b), the Arg471 variant leads to an addition of two new hydrogen bonds with Leu186 and Tyr192 (b′). The wild type amino acids are colored in pink, the variant amino acid is colored in green. c–c′ Glutamate (Glu) recognition by mGlu7 protein. Hydrogen atoms attached at the Cα atom of the ligand (Glu) are modeled with the corresponding ideal geometries. Dark green and light grey lines indicate hydrogen-bonding while light green lines indicate VDW contact. d–d′ The ligand-binding pocket. The orientation of Glutamate docked into the putative active site of mGlu7. d The structure of wild-type mGlu7. (d′) The structure of the Gly471Arg mutant