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| Title | Atomic Structure of the Cystic Fibrosis Transmembrane Conductance Regulator. |
|---|---|
| Journal, issue, pages | Cell, Vol. 167, Issue 6, Page 1586-11597.e9, Year 2016 |
| Publish date | Dec 1, 2016 |
 Authors | Zhe Zhang / Jue Chen /  |
| PubMed Abstract | The cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel evolved from the ATP-binding cassette (ABC) transporter family. In this study, we determined the structure of ...The cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel evolved from the ATP-binding cassette (ABC) transporter family. In this study, we determined the structure of zebrafish CFTR in the absence of ATP by electron cryo-microscopy to 3.7 Å resolution. Human and zebrafish CFTR share 55% sequence identity, and 42 of the 46 cystic-fibrosis-causing missense mutational sites are identical. In CFTR, we observe a large anion conduction pathway lined by numerous positively charged residues. A single gate near the extracellular surface closes the channel. The regulatory domain, dephosphorylated, is located in the intracellular opening between the two nucleotide-binding domains (NBDs), preventing NBD dimerization and channel opening. The structure also reveals why many cystic-fibrosis-causing mutations would lead to defects either in folding, ion conduction, or gating and suggests new avenues for therapeutic intervention. |
 External links | Cell / PubMed:27912062 |
| Methods | EM (single particle) |
| Resolution | 3.73 - 3.87 Å |
| Structure data | EMDB-8461: Structure of the cystic fibrosis transmembrane conductance regulator (CFTR) from zebrafish  EMDB-8516: |
| Chemicals |  ChemComp-D10: |
| Source |
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 Keywords | MEMBRANE PROTEIN / HYDROLASE / ABC transporter / anion channel / cystic fibrosis |
danio rerio (zebrafish)
Homo sapiens (human)
