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Structure and function of the CFTR chloride channel.
- Source :
-
Physiological reviews [Physiol Rev] 1999 Jan; Vol. 79 (1 Suppl), pp. S23-45. - Publication Year :
- 1999
-
Abstract
- Structure and Function of the CFTR Chloride Channel. Physiol. Rev. 79, Suppl.: S23-S45, 1999. - The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ABC transporter family that forms a novel Cl- channel. It is located predominantly in the apical membrane of epithelia where it mediates transepithelial salt and liquid movement. Dysfunction of CFTR causes the genetic disease cystic fibrosis. The CFTR is composed of five domains: two membrane-spanning domains (MSDs), two nucleotide-binding domains (NBDs), and a regulatory (R) domain. Here we review the structure and function of this unique channel, with a focus on how the various domains contribute to channel function. The MSDs form the channel pore, phosphorylation of the R domain determines channel activity, and ATP hydrolysis by the NBDs controls channel gating. Current knowledge of CFTR structure and function may help us understand better its mechanism of action, its role in electrolyte transport, its dysfunction in cystic fibrosis, and its relationship to other ABC transporters.
- Subjects :
- ATP-Binding Cassette Transporters metabolism
Adenosine Triphosphate metabolism
Amino Acid Sequence
Animals
Humans
Hydrolysis
Ion Channel Gating
Phosphorylation
Structure-Activity Relationship
Cystic Fibrosis Transmembrane Conductance Regulator chemistry
Cystic Fibrosis Transmembrane Conductance Regulator metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0031-9333
- Volume :
- 79
- Issue :
- 1 Suppl
- Database :
- MEDLINE
- Journal :
- Physiological reviews
- Publication Type :
- Academic Journal
- Accession number :
- 9922375
- Full Text :
- https://doi.org/10.1152/physrev.1999.79.1.S23