EC Number   |
General Information |
Reference |
|---|
   5.6.1.6 | evolution |
ATP-binding cassette (ABC) transporters are an ancient family of transmembrane proteins that utilize ATPase activity to move substrates across cell membranes. The ABCC subfamily of the ABC transporters includes active drug exporters and a unique ATP-gated ion channel, the cystic fibrosis transmembrane conductance regulator. CFTR channels and MRP efflux pumps share a conserved allosteric mechanism for coupling ATP binding to the translocation pathway, and reinforce the view that the CFTR gating mechanism is similar to the activation mechanisms of conventional ligand-gated channels. A proline (Pro355) at the base of pore-lining transmembrane segment 6 in enzyme CFTR is well conserved among the ABCC subfamily of ABC transporters |
734266 |
| 5.6.1.6 | evolution |
the enzyme belongs to the ATP-binding cassette (ABC) protein superfamily, ABCC subfamily, contains mainly transporters responsible for a range of functions from nutrient uptake to toxin export and these proteins are found in all organisms ranging from bacteria to mammals. The CFTR gene is unique within the ATP-binding cassette (ABC) protein family, predominantly of transporters, by coding a chloride channel |
733100 |
| 5.6.1.6 | evolution |
the enzyme is a bona fide member of the ATP-binding cassette (ABC) transporter superfamily. The presence of a gate in enzyme CFTR at a segment that may also serve as the selectivity filter provides functional duality of a restrictive segment close to the middle of the pore axis distinguishes CFTR from other members of the ABC protein family |
735191 |
| 5.6.1.6 | evolution |
the enzyme is a member of the ATP-binding cassette (ABC) transporter superfamily, a class of membrane proteins that couple the hydrolysis ofATPwith the transport of molecules across membranes. The enzyme belongs to the ABC-C subfamily (ABC-C7) |
734313 |
| 5.6.1.6 | evolution |
the enzyme is an ATP-binding cassette (ABC) adenylate kinase and anion channel in the ATP-binding cassette (ABC) transporter protein family |
734231 |
| 5.6.1.6 | malfunction |
a dysfunctional CFTR protein, e.g. by loss-of-function mutation, results in cystic fibrosis, a fatal pleiotropic disease, more than 1000 known mutations of this chloride channel result in a range of disease states. Cystic fibrosis is a Mendelian autosomal recessive disease of the young, due to its lethal nature in the early years of life, and affects roughly one in 2500 newborns with a total of 70000 people worldwide, pathophysiology, overview |
733100 |
| 5.6.1.6 | malfunction |
cystic fibrosis, one of the most common lethal genetic diseases, is caused by loss-of-function mutations of the cystic fibrosis transmembrane conductance regulator (CFTR) gene, which encodes a chloride channel. The third most common pathogenic mutation, a glycine-to-aspartate mutation at position 551 (G551D) shows a significantly decreased open probability caused by failure of the mutant channel to respond to ATP. The CFTR-targeted drug, VX-770 (Ivacaftor), which potentiates G551D-CFTR function in vitro by boosting its Po, is approved by the american food and drug administration to treat cystic fibrosis patients carrying this mutation |
734398 |
| 5.6.1.6 | malfunction |
dysfunctional enzyme causes the common lethal genetic disease cystic fibrosis |
734313 |
| 5.6.1.6 | malfunction |
enzyme mutations are the cause of cystsic fibrosis |
750278 |
| 5.6.1.6 | malfunction |
human bronchial airway epithelia derived from cystic fibrosis donors are homozygous for the F508del mutation in the enzyme |
734305 |
