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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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Bibliografski detalji
Izdano u:eLife
Glavni autori: Sorum, Ben, Töröcsik, Beáta, Csanády, László
Format: Artigo
Jezik:Inglês
Izdano: eLife Sciences Publications, Ltd 2017
Teme:
Online pristup: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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