Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
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Review
MeSH terms
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ATP-Binding Cassette Transporters / chemistry
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ATP-Binding Cassette Transporters / genetics
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ATP-Binding Cassette Transporters / metabolism*
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Adenosine Triphosphate / metabolism
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Animals
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Binding Sites
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Cystic Fibrosis / etiology
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Cystic Fibrosis / genetics
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Cystic Fibrosis / metabolism*
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Cystic Fibrosis Transmembrane Conductance Regulator / chemistry
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Cystic Fibrosis Transmembrane Conductance Regulator / genetics
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Cystic Fibrosis Transmembrane Conductance Regulator / metabolism*
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Humans
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Hydrolysis
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Ion Channel Gating
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Mutation
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Nucleotides / metabolism
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Phosphorylation
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Protein Conformation
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Protein Structure, Tertiary
Substances
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ATP-Binding Cassette Transporters
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CFTR protein, human
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Nucleotides
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Cystic Fibrosis Transmembrane Conductance Regulator
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Adenosine Triphosphate