Location of a permeant anion binding site in the cystic fibrosis transmembrane conductance regulator chloride channel pore

Hussein N. Rubaiy, Paul Linsdell

Résultat de recherche: Articleexamen par les pairs

13 Citations (Scopus)

Résumé

In the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel, lyotropic anions with high permeability also bind relatively tightly within the pore. However, the location of permeant anion binding sites, as well as their relationship to anion permeability, is not known. We have identified lysine residue K95 as a key determinant of permeant anion binding in the CFTR pore. Lyotropic anion binding affinity is related to the number of positively charged amino acids located in the inner vestibule of the pore. However, mutations that change the number of positive charges in this pore region have minimal effects on anion permeability. In contrast, a mutation at the narrow pore region alters permeability with minimal effects on anion binding. Our results suggest that a localized permeant anion binding site exists in the pore; however, anion binding to this site has little influence over anion permeability. Implications of this work for the mechanisms of anion recognition and permeability in CFTR are discussed.

Langue d'origineEnglish
Pages (de-à)233-241
Nombre de pages9
JournalJournal of Physiological Sciences
Volume65
Numéro de publication3
DOI
Statut de publicationPublished - mai 1 2015

Note bibliographique

Funding Information:
Acknowledgments We would like to thank Christina Irving and Dr. Yassine El Hiani for their assistance with this work. Supported by the Canadian Institutes of Health Research and Cystic Fibrosis Canada.

Publisher Copyright:
© 2015, The Physiological Society of Japan and Springer Japan.

ASJC Scopus Subject Areas

  • Physiology

PubMed: MeSH publication types

  • Journal Article
  • Research Support, Non-U.S. Gov't

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