Function of the R domain in the cystic fibrosis transmembrane conductance regulator chloride channel.

@article{Ma1997FunctionOT,
  title={Function of the R domain in the cystic fibrosis transmembrane conductance regulator chloride channel.},
  author={Jianjie Ma and Jiying Zhao and Mitchell L. Drumm and Junxia Xie and Pamela B. Davis},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 44},
  pages={28133-41}
}
For a cystic fibrosis transmembrane conductance regulator (CFTR) channel to enter its open state, serine residues in the R domain must be phosphorylated by cAMP-dependent protein kinase, and intracellular ATP must bind to the nucleotide-binding folds and subsequently be hydrolyzed. CFTR with its R domain partially removed, DeltaR(708-835)-CFTR, forms a chloride channel that opens independently of protein kinase A phosphorylation, with open probability approximately one-third that of the wild… CONTINUE READING

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