CFTR function, pathology and pharmacology at single-molecule resolution.

ABSTRACT: The cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel that regulates salt and fluid homeostasis across epithelial membranes¹. Alterations in CFTR cause cystic fibrosis, a fatal disease without a cure^2,3. Electrophysiological properties of CFTR have been analysed for decades^4-6. The structure of CFTR, determined in two globally distinct conformations, underscores its evolutionary relationship with other ATP-binding cassette transporters. However, direct correlations between the essential functions of CFTR and extant structures are lacking at present. Here we combine ensemble functional measurements, single-molecule fluorescence resonance energy transfer, electrophysiology and kinetic simulations to show that the two nucleotide-bi

SUBMITTER: Levring J 

PROVIDER: S-EPMC10115640 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature