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Strict coupling between CFTR’s catalytic cycle and gating of its Cl(−) ion pore revealed by distributions of open channel burst durations
CFTR, the ABC protein defective in cystic fibrosis, functions as an anion channel. Once phosphorylated by protein kinase A, a CFTR channel is opened and closed by events at its two cytosolic nucleotide binding domains (NBDs). Formation of a head-to-tail NBD1/NBD2 heterodimer, by ATP binding in two i...
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| Autori principali: | , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
2009
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2824283/ https://ncbi.nlm.nih.gov/pubmed/19966305 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0911061107 |
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