Conformational dynamics in TRPV1 channels reported by an encoded coumarin amino acid.

ABSTRACT: TRPV1 channels support the detection of noxious and nociceptive input. Currently available functional and structural data suggest that TRPV1 channels have two gates within their permeation pathway: one formed by a 'bundle-crossing' at the intracellular entrance and a second constriction at the selectivity filter. To describe conformational changes associated with channel gating, the fluorescent non-canonical amino acid coumarin-tyrosine was genetically encoded at Y671, a residue proximal to the selectivity filter. Total internal reflection fluorescence microscopy was performed to image the conformational dynamics of the channels in live cells. Photon counts and optical fluctuations from coumarin encoded within TRPV1 tetramers correlates with channel activation by capsaicin, providing an op

SUBMITTER: Steinberg X 

PROVIDER: S-EPMC5716661 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature