Fig. 3: GSK1702934A binding sites in hTRPC3.
From: Structural mechanism of the agonist binding on human TRPC3 channel
a, b Cryo-EM density maps of GSK1702934A-bound state hTRPC3 shown in side view (a) and top view (b). Subunits A, B, C, and D are colored in yellow, blue, pink, and green, respectively. Ligand GSK1702934A is colored in gold. The approximate boundary of the cell membrane is indicated by gray lines. TMD transmembrane domain, ICD intracellular cytosolic domain. c Densities of GSK1702934A and nearby residues shown in side view. Densities are shown as grey surfaces. GSK1702934A is shown as sticks, and hTRPC3 is shown as cartoon. Both are colored the same as in (a). d, e Close-up view of the GSK1702934A-binding site. The GSK1702934A molecule and the side chains of its interacting residues are shown as sticks. f Cartoon representation of the interactions between GSK1702934A and hTRPC3. S6 of subunit A and S5, S6, pore helices of subunit B are represented as yellow ovals and blue ovals, respectively. Residues that interact with GSK1702934A are labeled inside the ovals. g Sequence alignment among TRPC1/4/5 and TRPC3/6/7 is shown. The residues that interact with GSK1702934A are marked by gold asterisks. Conserved residues are colored in gold. The corresponding domains are labeled above the sequence.
