Different Ligands of the TRPV3 Cation Channel Cause Distinct Conformational Changes as Revealed by Intrinsic Tryptophan Fluorescence Quenching
TLDR Different ligands change the shape of the TRPV3 ion channel in unique ways.
The study investigated the effects of various ligands on the TRPV3 cation channel using intrinsic tryptophan fluorescence quenching, revealing that camphor, eucalyptol, and icilin caused significant conformational changes, while menthol did not. The research demonstrated that different ligands modulated TRPV3 through distinct mechanisms, with specific interactions and structural rearrangements. The findings provided valuable insights into the structural dynamics and regulatory processes of TRPV3, contributing to the understanding of its physiological functions and potential as a therapeutic target.
