Sequence and structural conservation reveal fingerprint residues in TRP channels.

ABSTRACT: Transient receptor potential (TRP) proteins are a large family of cation-selective channels, surpassed in variety only by voltage-gated potassium channels. Detailed molecular mechanisms governing how membrane voltage, ligand binding, or temperature can induce conformational changes promoting the open state in TRP channels are still a matter of debate. Aiming to unveil distinctive structural features common to the transmembrane domains within the TRP family, we performed phylogenetic reconstruction, sequence statistics, and structural analysis over a large set of TRP channel genes. Here, we report an exceptionally conserved set of residues. This fingerprint is composed of twelve residues localized at equivalent three-dimensional positions in TRP channels from the different subtypes. Moreove

SUBMITTER: Cabezas-Bratesco D 

PROVIDER: S-EPMC9242649 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature