The ABC protein turned chloride channel whose failure causes cystic fibrosis.
CFTR chloride channels are encoded by the gene mutated in patients with cystic fibrosis. These channels belong to the superfamily of ABC transporter ATPases. ATP-driven conformational changes, which in other ABC proteins fuel uphill substrate transport across cellular membranes, in CFTR open and close a gate to allow transmembrane flow of anions down their electrochemical gradient. New structural and biochemical information from prokaryotic ABC proteins and functional information from CFTR channels has led to a unifying mechanism explaining those ATP-driven conformational changes.
Gadsby
David C
DC
Laboratory of Cardiac/Membrane Physiology, The Rockefeller University, New York, NY 10021, USA. gadsby@rockefeller.edu
Vergani
Paola
P
Csanády
László
L
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D003550:Cystic Fibrosis / Q000209:etiology / Q000235:genetics / Q000378:metabolism*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D015640:Ion Channel Gating; D009154:Mutation; D009711:Nucleotides / Q000378:metabolism; D010766:Phosphorylation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D018528:ATP-Binding Cassette Transporters; C505032:CFTR protein, human; D009711:Nucleotides; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D000255:Adenosine Triphosphate