Probing the structural and functional domains of the CFTR chloride channel

Myles H. Akabas, Min Cheung, Romain Guinamard

Research output: Contribution to journalShort surveypeer-review

13 Scopus citations


The cystic fibrosis transmembrane conductance regulator (CFTR) forms an anion-selective channel involved in epithelial chloride transport. Recent studies have provided new insights into the structural determinants of the channel's functional properties, such as anion selectivity, single-channel conductance, and gating. Using the scanning-cysteine-accessibility method we identified 7 residues in the MI membrane-spanning segment and 1l residues in and flanking the M6 segment that are exposed on the water-accessible surface of the protein; many of these residues may line the ion-conducting pathway. The pattern of the accessible residues suggests that these segments have a largely α-helical secondary structure with one face exposed in the channel lumen. Our results suggest that the residues at the cytoplasmic end of the M6 segment loop back into the channel, narrowing the lumen, and thereby forming both the major resistance to ion movement and the charge-selectivity filter.

Original languageEnglish (US)
Pages (from-to)453-463
Number of pages11
JournalJournal of Bioenergetics and Biomembranes
Issue number5
StatePublished - 1997
Externally publishedYes


  • ATP-binding cassette transporter
  • Cysteine
  • Ion channel
  • Ion selectivity
  • MDR
  • Methanethiosulfonate
  • Periptasmic permease
  • STE6
  • TAP

ASJC Scopus subject areas

  • Physiology
  • Cell Biology


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