CFTR structure and cystic fibrosis

Natasha Cant; Naomi Pollock; Robert C Ford

doi:10.1016/j.biocel.2014.02.004

CFTR structure and cystic fibrosis

Int J Biochem Cell Biol. 2014 Jul:52:15-25. doi: 10.1016/j.biocel.2014.02.004. Epub 2014 Feb 15.

Authors

Natasha Cant¹, Naomi Pollock¹, Robert C Ford²

Affiliations

¹ University of Manchester, Faculty of Life Sciences, Michael Smith Building, Manchester M13 9PT, UK.
² University of Manchester, Faculty of Life Sciences, Michael Smith Building, Manchester M13 9PT, UK. Electronic address: robert.ford@manchester.ac.uk.

PMID: 24534272
DOI: 10.1016/j.biocel.2014.02.004

Abstract

CFTR (cystic fibrosis transmembrane conductance regulator) is a member of the ATP-binding cassette family of membrane proteins. Although almost all members of this family are transporters, CFTR functions as a channel with specificity for anions, in particular chloride and bicarbonate. In this review we look at what is known about CFTR structure and function within the context of the ATP-binding cassette family. We also review current strategies aimed at obtaining the high resolution structure of the protein.

Keywords: CFTR; Cystic fibrosis; Ion channel; Membrane protein; Protein structure.

Publication types

Review

MeSH terms

Cystic Fibrosis / genetics
Cystic Fibrosis / metabolism*
Cystic Fibrosis Transmembrane Conductance Regulator / chemistry*
Cystic Fibrosis Transmembrane Conductance Regulator / genetics
Cystic Fibrosis Transmembrane Conductance Regulator / metabolism*
Humans
Models, Molecular
Protein Structure, Secondary

Substances

Cystic Fibrosis Transmembrane Conductance Regulator