Structural insights into the gating mechanism of human SLC26A9 mediated by its C-terminal sequence.

ABSTRACT: The human SLC26 transporter family exhibits various transport characteristics, and family member SLC26A9 performs multiple roles, including acting as Cl^-/HCO₃^- exchangers, Cl^- channels, and Na⁺ transporters. Some mutations of SLC26A9 are correlated with abnormalities in respiration and digestion systems. As a potential target colocalizing with CFTR in cystic fibrosis patients, SLC26A9 is of great value in drug development. Here, we present a cryo-EM structure of the human SLC26A9 dimer at 2.6 Å resolution. A segment at the C-terminal end is bound to the entry of the intracellular vestibule of the putative transport pathway, which has been proven by electrophysiological experiments to be a gating modulator. Multiple chloride and sodium

SUBMITTER: Chi X 

PROVIDER: S-EPMC7417587 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature