Fig. 1: Structure of human TRPC5 in complex with Pico145. | Communications Biology

Fig. 1: Structure of human TRPC5 in complex with Pico145.

From: Human TRPC5 structures reveal interaction of a xanthine-based TRPC1/4/5 inhibitor with a conserved lipid binding site

Fig. 1

a Cryo-EM density map of TRPC5:Pico145 (contour level: 0.0373). b Model of TRPC5:Pico145 coloured by monomer, showing the typical TRP channel domain swap architecture. Dashed lines indicate the predicted position of the lipid bilayer. Insets show one of the four Pico145-binding sites (between trans-membrane domains of the blue and orange TRPC5 monomers) and one of the four putative intracellular zinc-binding sites (in the magenta monomer). c Representative fit of TRPC5:Pico145 model b into the experimental density a showing helical regions spanning residues 193–234 (contour level: 0.0423).

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