Nonintegral stoichiometry in CFTR gating revealed by a pore-lining mutation.

ABSTRACT: Cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ATP-binding cassette (ABC) protein superfamily. Unlike most other ABC proteins that function as active transporters, CFTR is an ATP-gated chloride channel. The opening of CFTR's gate is associated with ATP-induced dimerization of its two nucleotide-binding domains (NBD1 and NBD2), whereas gate closure is facilitated by ATP hydrolysis-triggered partial separation of the NBDs. This generally held theme of CFTR gating-a strict coupling between the ATP hydrolysis cycle and the gating cycle-is put to the test by our recent finding of a short-live

SUBMITTER: Jih KY 

PROVIDER: S-EPMC3457689 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature