Annals of Thoracic Medicine Official publication of the Saudi Thoracic Society, affiliated to King Saud University
 
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REVIEW ARTICLE
Year : 2012  |  Volume : 7  |  Issue : 3  |  Page : 115-121

Role of ATP binding and hydrolysis in the gating of the cystic fibrosis transmembrane conductance regulator


University of Cambridge School of Clinical Medicine, Addenbrookes's Hospital, Cambridge, CB2 0SP, United Kingdom

Correspondence Address:
Taras Gout
Sherwood Room Letterboxes, University of Cambridge School of Clinical Medicine, Addenbrookes's Hospital, Box 111, Hills Road, Cambridge, CB2 0SP
United Kingdom
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DOI: 10.4103/1817-1737.98842

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The CFTR gene is unique within the ATP-binding cassette (ABC) protein family, predominantly of transporters, by coding a chloride channel. The gating mechanism of ABC proteins has been characterized by the ATP Switch model in terms cycles of dimer formation and dissociation linked to ATP binding and hydrolysis, respectively. It would be of interest to assess the extent that Cystic Fibrosis Transmembrane Conductance Regulator (CFTR), a functional channel, fits the ATP Switch model for ABC transporters. Additional transporter mechanisms, namely those of Pgp and HlyB, are discussed for perspective. Literature search of databases selected key references in comparing and contrasting the gating mechanism. CFTR is a functional chloride channel facilitating transmembrane anion flow down electrochemical gradients. A dysfunctional CFTR protein results in cystic fibrosis, a fatal pleiotropic disease currently managed symptomatically. Understanding the gating mechanism will help target drug development aimed at alleviating and curing the disease.


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