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| Title | Molecular Structure of the Human CFTR Ion Channel. |
|---|---|
| Journal, issue, pages | Cell, Vol. 169, Issue 1, Page 85-95.e8, Year 2017 |
| Publish date | Mar 23, 2017 |
 Authors | Fangyu Liu / Zhe Zhang / László Csanády / David C Gadsby / Jue Chen /   |
| PubMed Abstract | The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of ...The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of dephosphorylated human CFTR without nucleotides, determined by electron cryomicroscopy (cryo-EM). Close resemblance of this human CFTR structure to zebrafish CFTR under identical conditions reinforces its relevance for understanding CFTR function. The human CFTR structure reveals a previously unresolved helix belonging to the R domain docked inside the intracellular vestibule, precluding channel opening. By analyzing the sigmoid time course of CFTR current activation, we propose that PKA phosphorylation of the R domain is enabled by its infrequent spontaneous disengagement, which also explains residual ATPase and gating activity of dephosphorylated CFTR. From comparison with MRP1, a feature distinguishing CFTR from all other ABC transporters is the helix-loop transition in transmembrane helix 8, which likely forms the structural basis for CFTR's channel function. |
 External links | Cell / PubMed:28340353 |
| Methods | EM (single particle) |
| Resolution | 3.87 Å |
| Structure data |  PDB-5uak: |
| Source |
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 Keywords |  MEMBRANE PROTEIN / HYDROLASE / ABC transporter / anion channel / cystic fibrosis |
