title: On the structural organization of the intracellular domains of CFTR.
abstract: 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.
authors: Instituto di Biofisica, CNR, Via de Marini, 6, 16149 Genova, Italy. Electronic address: oscar.moran@cnr.it.
authors: Oscar
authors: O
authors: Moran
mesh_terms: D003550:Cystic Fibrosis / Q000235:genetics / Q000378:metabolism*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D010766:Phosphorylation; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D019005:Cystic Fibrosis Transmembrane Conductance Regulator
keywords: CFTR; Cystic fibrosis; NBD; Regulatory domain; Structure