Abstract
Coordination of membrane lipids preserves structural integrity and subsidizes regulatory functions of channel complexes. Transient receptor potential canonical 3 (TRPC3) channel is a tetrameric and non-selective cation channel, which is directly activated by diacylglycerols (DAGs). Recent single-particle cryo-EM studies identified two key lipid interaction sites named L1 and L2, which can accommodate DAGs. To delve into the role of L1 and L2 in TRPC3 regulation, we combined electrophysiology with site-directed mutagenesis guided by molecular dynamics (MD) simulations.
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