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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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Bibliografische gegevens
Gepubliceerd in:eLife
Hoofdauteurs: Sorum, Ben, Töröcsik, Beáta, Csanády, László
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: eLife Sciences Publications, Ltd 2017
Onderwerpen:
Online toegang: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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