The ABC protein turned chloride channel whose failure causes cystic fibrosis

David C. Gadsby (), Paola Vergani and László Csanády
Additional contact information
David C. Gadsby: Laboratory of Cardiac/Membrane Physiology, The Rockefeller University
Paola Vergani: University College London
László Csanády: Semmelweis University, 1444 Budapest, Pf. 262

Nature, 2006, vol. 440, issue 7083, 477-483

Abstract: 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.

Date: 2006
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DOI: 10.1038/nature04712

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