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Author Notes:

To whom correspondence should be addressed: Division of Pulmonology, Allergy/Immunology, Cystic Fibrosis, and Sleep, Department of Pediatrics, Center for Cystic Fibrosis Research, Emory University School of Medicine and Children's Healthcare of Atlanta, 2015 Uppergate Dr., Atlanta, GA 30322. Tel.: 404-727-3654; Fax: 404-712-0920; E-mail: namccar@emory.edu.


Research Funding:

This work was supported, in whole or in part, by National Institutes of Health Grant R01-DK056481 (to N. M.).


  • ABC Transporter
  • CFTR
  • Gating
  • Oocyte
  • Xenopus
  • MTS Reagents
  • Pore
  • Salt Bridge

Two Salt Bridges Differentially Contribute to the Maintenance of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Channel Function


Journal Title:

Journal of Biological Chemistry


Volume 288, Number 28


, Pages 20758-20767

Type of Work:

Article | Final Publisher PDF


Background: Two salt bridges, Arg347–Asp924 and Arg352–Asp993, have been identified in CFTR, but the timing of their interaction remains unknown. Results: Arg347-Asp924-Asp993 form a triangular salt bridge and work together with the Arg352-Asp993 salt bridge to maintain the open pore architecture of CFTR. Conclusion: These salt bridge residues interact and contribute differently in stabilizing the open pore during gating cycle. Significance: Understanding the CFTR pore dynamic open-closed transition is crucial for rational drug design.

Copyright information:

© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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