Open AccessRole of ATP binding and hydrolysis in the gating of the cystic fibrosis transmembrane conductance regulator
Author(s) -
Taras Gout
Publication year - 2012
Publication title -
annals of thoracic medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.639
H-Index - 33
eISSN - 1817-1737
pISSN - 1998-3557
DOI - 10.4103/1817-1737.98842
Subject(s) - cystic fibrosis transmembrane conductance regulator , gating , chloride channel , atp binding cassette transporter , atp hydrolysis , transmembrane protein , transporter , regulator , microbiology and biotechnology , biophysics , ion channel , biochemistry , cystic fibrosis , chemistry , medicine , biology , gene , enzyme , receptor , atpase
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.