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CFTR: what's it like inside the pore?

Xuehong Liu1, Stephen S Smith, David C Dawson

  • 1Department of Physiology/Pharmacology, Oregon Health & Science University, Portland, Oregon 97239, USA. liuxu@ohsu.edu

Journal of Experimental Zoology. Part A, Comparative Experimental Biology
|November 5, 2003
PubMed
Summary

The Cystic Fibrosis Conductance Regulator (CFTR) channel

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Area of Science:

  • Ion channel structure and function
  • Molecular biophysics
  • Membrane transport

Background:

  • The Cystic Fibrosis Conductance Regulator (CFTR) is a cAMP-activated anion channel.
  • The precise mechanism of anion permeation through CFTR remains unclear.
  • Understanding CFTR's pore environment is crucial for elucidating its function.

Purpose of the Study:

  • To investigate the structural basis of anion permeation in the CFTR channel.
  • To characterize the environment experienced by anions within the CFTR pore.
  • To identify key residues involved in anion conduction.

Main Methods:

  • Analysis of anion permeability and binding selectivity.
  • Modeling of the CFTR pore as a dielectric tunnel.
  • Covalent labeling of engineered cysteines.
  • pH titration of engineered cysteines and histidines.

Main Results:

  • CFTR anion permeation and selectivity align with a dielectric tunnel model.
  • Anion partitioning between water and a polarizable space (dielectric constant ~19) explains selectivity.
  • Covalent labeling and pH titration reveal a positively charged outer vestibule.
  • Residue R334 in TM6 contributes to the positive electrostatic potential in the outer vestibule, enhancing anion conduction.

Conclusions:

  • The CFTR pore environment facilitates anion permeation through a dielectric tunnel mechanism.
  • A positively charged outer vestibule, influenced by R334, plays a key role in CFTR anion conduction.
  • These findings provide structural insights into CFTR channel function and anion transport.

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