Conformational changes in a pore-lining helix coupled to cystic fibrosis transmembrane conductance regulator channel gating.

@article{Beck2008ConformationalCI,
  title={Conformational changes in a pore-lining helix coupled to cystic fibrosis transmembrane conductance regulator channel gating.},
  author={Edward J. Beck and Yu Kyung Yang and Sirin Yaemsiri and Viswanathan Raghuram},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 8},
  pages={4957-66}
}
Cystic fibrosis transmembrane conductance regulator (CFTR), the protein dysfunctional in cystic fibrosis, is unique among ATP-binding cassette transporters in that it functions as an ion channel. In CFTR, ATP binding opens the channel, and its subsequent hydrolysis causes channel closure. We studied the conformational changes in the pore-lining sixth transmembrane segment upon ATP binding by measuring state-dependent changes in accessibility of substituted cysteines to methanethiosulfonate… CONTINUE READING