On the structural organization of the intracellular domains of CFTR

The cystic fibrosis transmembrane conductance regulator (CFTR) is a multidomain membrane protein forming an anion selective channel. Mutations in the gene encoding CFTR cause cystic fibrosis (CF). The intracellular side of CFTR constitutes about 80% of the total mass of the protein. This region incl...

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Veröffentlicht in:The international journal of biochemistry & cell biology 2014-07, Vol.52, p.7-14
1. Verfasser: Moran, Oscar
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description The cystic fibrosis transmembrane conductance regulator (CFTR) is a multidomain membrane protein forming an anion selective channel. Mutations in the gene encoding CFTR cause cystic fibrosis (CF). The intracellular side of CFTR constitutes about 80% of the total mass of the protein. This region includes domains involved in ATP-dependent gating and regulatory protein kinase-A phosphorylation sites. The high-resolution molecular structure of CFTR has not yet been solved. However, a range of lower resolution structural data, as well as functional biochemical and electrophysiological data, are now available. This information has enabled the proposition of a working model for the structural architecture of the intracellular domains of the CFTR protein. This article is part of a Directed Issue entitled: Cystic Fibrosis: From o-mics to cell biology, physiology, and therapeutic advances.
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identifier ISSN: 1357-2725
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source MEDLINE; Elsevier ScienceDirect Journals
subjects Biochemistry
Biology
CFTR
Channels
Cystic fibrosis
Cystic Fibrosis - genetics
Cystic Fibrosis - metabolism
Cystic Fibrosis Transmembrane Conductance Regulator - chemistry
Cystic Fibrosis Transmembrane Conductance Regulator - genetics
Cystic Fibrosis Transmembrane Conductance Regulator - metabolism
Encoding
Humans
Models, Molecular
Molecular structure
NBD
Phosphorylation
Physiology
Protein Binding
Protein Structure, Tertiary
Proteins
Regulatory domain
Structure
title On the structural organization of the intracellular domains of CFTR
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