Anno2014
AutoriMoran O.
AbstractThe 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. © 2014 Elsevier Ltd.
RivistaInternational Journal Of Biochemistry & Cell Biology
ISSN1357-2725
Impact factor0
Volume52
Pagina inizio7
Pagina fine14
Autori IBFOscar MORAN
Linee di Ricerca IBFMD.P01.009.001
Sedi IBFIBF.GE