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Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions

CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, is opened by ATP binding to two cytosolic nucleotide binding domains (NBDs), but pore-domain mutations may also impair gating. ATP-bound NBDs dimerize occluding two nucleotides at interfacial binding sites; one site hydrolyzes ATP,...

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Détails bibliographiques
Publié dans:eLife
Auteurs principaux: Sorum, Ben, Töröcsik, Beáta, Csanády, László
Format: Artigo
Langue:Inglês
Publié: eLife Sciences Publications, Ltd 2017
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC5626490/
https://ncbi.nlm.nih.gov/pubmed/28944753
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.29013
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