Fig. 1: 3D reconstructions and atomic models of TRPM3APO and of TRPM3 in the presence of antagonists.
From: Stereoselectivity and functional plasticity of a common ligand-binding pocket in TRPM3
a Representative chromatogram from a single size exclusion chromatography run of TRPM3 (left) and SDS-PAGE analysis of the peak fraction at 6.5 minutes from the same run. b Chemical drawings of primidone, isosakuranetin and ononetin. c Overall structures of TRPM3 bound to primidone (violet blue), isosakuranetin (violet), ononetin (wheat) and in the apo-state (marine) displayed as surface representation with one subunit shown as cylinders. Contouration in ChimeraX is at 0.039, 0.062, 0.061 and 0.113 σ for primidone, isosakuranetin, ononetin and the apo-state, respectively. d Close-up view from the side on the VSLD ligand binding pocket with ligands and interacting residues lining S1-S4 shown as sticks. e Close-up views on the ligand binding sites are shown with important interactions highlighted as dashed lines; hydrogen bonds in black; salt bridges in pink; cation-π stacking in green and π-π stackings in cyan. Hydrophobic contacts are not specifically marked. Residues that have been mutated in this study are labelled in red. In d and e colors are as in c. Source data are provided as a Source Data file.
