Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations.

@article{Csandy2010StrictCB,
  title={Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations.},
  author={L{\'a}szl{\'o} Csan{\'a}dy and Paola Vergani and David C. Gadsby},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 3},
  pages={1241-6}
}
CFTR, the ABC protein defective in cystic fibrosis, functions as an anion channel. Once phosphorylated by protein kinase A, a CFTR channel is opened and closed by events at its two cytosolic nucleotide binding domains (NBDs). Formation of a head-to-tail NBD1/NBD2 heterodimer, by ATP binding in two interfacial composite sites between conserved Walker A and B motifs of one NBD and the ABC-specific signature sequence of the other, has been proposed to trigger channel opening. ATP hydrolysis at the… CONTINUE READING