Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization
Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization
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England: eLife Sciences Publications Ltd
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English
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England: eLife Sciences Publications Ltd
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In CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, ATP-binding-induced dimerization of two cytosolic nucleotide binding domains (NBDs) opens the pore, and dimer disruption following ATP hydrolysis closes it. Spontaneous openings without ATP are rare in wild-type CFTR, but in certain CF mutants constitute the only gating mechani...
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Full title
Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization
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TN_cdi_doaj_primary_oai_doaj_org_article_bbe2db8f8067467da9c69baa9c7a6322
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bbe2db8f8067467da9c69baa9c7a6322
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ISSN
2050-084X
E-ISSN
2050-084X
DOI
10.7554/eLife.18164
