Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR.

  title={Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR.},
  author={A. Aleksandrov and Pradeep Kota and L. Cui and Tim Jensen and A. Alekseev and Santiago Reyes and L. He and M. Gentzsch and L. Aleksandrov and N. Dokholyan and J. Riordan},
  journal={Journal of molecular biology},
  volume={419 1-2},
  • A. Aleksandrov, Pradeep Kota, +8 authors J. Riordan
  • Published 2012
  • Biology, Medicine
  • Journal of molecular biology
  • Most cystic fibrosis is caused by a deletion of a single residue (F508) in CFTR (cystic fibrosis transmembrane conductance regulator) that disrupts the folding and biosynthetic maturation of the ion channel protein. Progress towards understanding the underlying mechanisms and overcoming the defect remains incomplete. Here, we show that the thermal instability of human ΔF508 CFTR channel activity evident in both cell-attached membrane patches and planar phospholipid bilayers is not observed in… CONTINUE READING

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    Publications referenced by this paper.
    Regulatory insertion removal restores maturation, stability and function of DeltaF508 CFTR.
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    Domain interdependence in the biosynthetic assembly of CFTR.
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    Thermally Unstable Gating of the Most Common Cystic Fibrosis Mutant Channel (ΔF508)
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