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Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization
In CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, ATP-binding-induced dimerization of two cytosolic nucleotide binding domains (NBDs) opens the pore, and dimer disruption following ATP hydrolysis closes it. Spontaneous openings without ATP are rare in wild-type CFTR, but in cer...
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| Vydáno v: | eLife |
|---|---|
| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
eLife Sciences Publications, Ltd
2016
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4956468/ https://ncbi.nlm.nih.gov/pubmed/27328319 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.18164 |
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