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J Cyst Fibros. 2018 Mar;17(2S):S5-S8. doi: 10.1016/j.jcf.2017.08.008. Epub 2017 Aug 31.

CFTR structure.

Author information

1
IMPMC, Sorbonne Universités - UPMC Université Paris 06, UMR CNRS 7590, Muséum National d'Histoire Naturelle, IRD UMR 206, 4 Place Jussieu, Paris, France. Electronic address: isabelle.callebaut@impmc.upmc.fr.
2
Molecular Medicine, The Hospital for Sick Children, Toronto M5G 0A4, Canada.
3
Molecular Medicine, The Hospital for Sick Children, Toronto M5G 0A4, Canada; Department of Biochemistry, University of Toronto, Toronto M5G 1X8, Canada.

Abstract

Structural studies of the cystic fibrosis transmembrane conductance regulator (CFTR) protein are critical to understand molecular mechanisms involved in gating of the apical anion channel as well as the way in which the gating is regulated, especially by the regulatory region (R region). They are also instrumental for understanding the root cause of cystic fibrosis (CF) and supporting the development of therapeutic strategies. In this short review, we summarize recent progress in the knowledge of the CFTR 3D structure and briefly discuss implications for CF drug development.

KEYWORDS:

3D structure; CFTR; Cryo-EM; Molecular modeling; NMR

PMID:
28866450
DOI:
10.1016/j.jcf.2017.08.008

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