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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,...
Tallennettuna:
| Julkaisussa: | eLife |
|---|---|
| Päätekijät: | , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
eLife Sciences Publications, Ltd
2017
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| Aiheet: | |
| Linkit: | 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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