Locating a plausible binding site for an open-channel blocker, GlyH-101, in the pore of the cystic fibrosis transmembrane conductance regulator.

@article{Norimatsu2012LocatingAP,
  title={Locating a plausible binding site for an open-channel blocker, GlyH-101, in the pore of the cystic fibrosis transmembrane conductance regulator.},
  author={Yohei Norimatsu and Anthony Ivetac and Christopher Alexander and Nicolette O'Donnell and Leah L. Frye and Mark S. P. Sansom and David C. Dawson},
  journal={Molecular pharmacology},
  year={2012},
  volume={82 6},
  pages={
          1042-55
        }
}
High-throughput screening has led to the identification of small-molecule blockers of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel, but the structural basis of blocker binding remains to be defined. We developed molecular models of the CFTR channel on the basis of homology to the bacterial transporter Sav1866, which could permit blocker binding to be analyzed in silico. The models accurately predicted the existence of a narrow region in the pore that is a… CONTINUE READING

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