Fig. 2: The binding site of DAG on hTRPC3.
From: Structural mechanism of the agonist binding on human TRPC3 channel
a The content of 1,2-dioleoyl-sn-glycerol in hTRPC3 protein sample and buffer control. hTRPC3 protein was purified using amylose resin and subsequently buffer-exchanged by ultrafiltration. The data are shown as the mean ± SD. The number of the analyzed TRPC3 protein sample is 4 and the number of buffer control sample is 2, biological replicates. The data were analyzed using one-tailed t-test and the p-value is 0.0049. Source data are provided as a Source Data file. b The electron density of the DAG and nearby residues shown in the semi-transparent surface. c The close-up view of the DAG-binding pocket of hTRPC3. DAG is shown as sticks, and hTRPC3 is shown as cartoon. d Cartoon representation of the interactions between hTRPC3 and DAG. The dashed lines represent the regions that were not modeled due to their flexibility. e Sequence alignment among TRPC1/4/5 and TRPC3/6/7 is shown. The residues that interact with DAG are marked by light green asterisks. Conserved residues are colored in light green. The corresponding domains are labeled above the sequence.
