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• W1971736406 startingPage "693" @default.
• W1971736406 abstract "As the product of the gene mutated in cystic fibrosis, the most common genetic disease of Caucasians, CFTR is an atypical ABC protein. From an evolutionary perspective, it is apparently a relatively young member of the ABC family, present only in metazoans where it plays a critical role in epithelial salt and fluid homeostasis. Functionally, the membrane translocation process it mediates, the passive bidirectional diffusion of small inorganic anions, is simpler than the vectorial transport of larger more complex substrates (allocrites) by most ABC transporters. However, the control of the permeation pathway which cannot go unchecked is necessarily more stringent than in the case of the transporters. There is tight regulation by the phosphorylation/dephosphorylation of the unique CFTR R domain superimposed on the basic ABC regulation mode of ATP binding and hydrolysis at the dual nucleotide binding sites. As with other ABCC subfamily members, only the second of these sites is hydrolytic in CFTR. The phosphorylation and ATP binding/hydrolysis events do not strongly influence each other; rather, R domain phosphorylation appears to enable transduction of the nucleotide binding allosteric signal to the responding channel gate. ATP hydrolysis is not required for either the opening or closing gating transitions but efficiently clears the ligand-binding site enabling a new gating cycle to be initiated." @default.
• W1971736406 created "2016-06-24" @default.
• W1971736406 creator A5023676292 @default.
• W1971736406 creator A5026175544 @default.
• W1971736406 creator A5049400835 @default.
• W1971736406 date "2006-09-26" @default.
• W1971736406 modified "2023-09-26" @default.
• W1971736406 title "CFTR (ABCC7) is a hydrolyzable-ligand-gated channel" @default.
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• W1971736406 doi "https://doi.org/10.1007/s00424-006-0140-z" @default.
• W1971736406 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17021796" @default.
• W1971736406 hasPublicationYear "2006" @default.
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