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

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

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 cer...

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Bibliographic Details
Main Authors: Csaba Mihályi, Beáta Töröcsik, László Csanády
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2016-06-01
Series:eLife
Subjects:
mutant cycle
thermodynamic coupling
ABC protein
structure
conformation
Online Access:https://elifesciences.org/articles/18164

Internet

https://elifesciences.org/articles/18164

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