Dataset Information
Cryo-EM structure of mouse TRPV3 in a nanodisc
Ontology highlight
ABSTRACT:
SUBMITTER: Osamu Nureki
PROVIDER: EMPIAR-10400 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
The structure of lipid nanodisc-reconstituted TRPV3 reveals the gating mechanism.
Nature structural & molecular biology 20200622 7
Transient receptor potential vanilloid subfamily member 3 (TRPV3) is a temperature-sensitive cation channel. Previous cryo-EM analyses of TRPV3 in detergent micelles or amphipol proposed that the lower gate opens by α-to-π helical transitions of the nearby S6 helix. However, it remains unclear how physiological lipids are involved in the TRPV3 activation. Here we determined the apo state structure of mouse (Mus musculus) TRPV3 in a lipid nanodisc at 3.3 Å resolution. The structure revealed that ...[more]
