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Article

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

21 Jun 2016

Abstract excerpt

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 mechanism, stimulated by ivacaftor, a clinically approved CFTR...

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PMID: 27328319
DOI: 10.7554/elife.18164

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