Abstract
In recent years a new family of transport proteins called ABS transporters has emerged. One member of this novel family, called CFTR (cystic fibrosis transmembrane conductance regulator), has received special attention because of its association with the disease cystic fibrosis (CF). This is an inherited disorder affecting about 1 in 2000 Caucasians by impairing epithelial ion transport, particularly that of chloride. Death may occur in severe cases because of chronic lung infections, especially by Pseudomonas aeruginosa, which cause a slow decline in pulmonary function. The prospects of ameliorating the symptoms of CF and even curing the disease were greatly heightened in 1989 following the cloning of the CFTR gene and the discovery that the mutation (ΔF508), which causes most cases of CF, is localized within a putative ATP binding/ATP hydrolysis domain. The purpose of this introductory review in this minireview series is to summarize what we and others have learned during the past eight years about the structure and function of the first nucleotide binding domain (NBFI or NBDI) of the CFTR protein and the effect thereon of disease-causing mutations. The relationship of these new findings to the pathogenesis of CF is also discussed.
Original language | English (US) |
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Pages (from-to) | 417-427 |
Number of pages | 11 |
Journal | Journal of Bioenergetics and Biomembranes |
Volume | 29 |
Issue number | 5 |
DOIs | |
State | Published - 1997 |
Externally published | Yes |
Keywords
- ATPase
- CFTR
- Cystic fibrosis
- Genetic disease
- Lung infections
- Nucleotide binding domain
- Pathogenesis
- Pseudomonas aeruginosa
ASJC Scopus subject areas
- Physiology
- Cell Biology