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Structure paper

TitleA topological switch in CFTR modulates channel activity and sensitivity to unfolding.
Journal, issue, pagesNat. Chem. Biol., Vol. 17, Page 989-997, Year 2021
Publish dateJun 15, 2020 (structure data deposition date)
AuthorsScholl, D. / Sigoillot, M. / Overtus, M. / Martinez, R.C. / Martens, C. / Wang, Y. / Pardon, E. / Laeremans, T. / Garcia-Pino, A. / Steyaert, J. ...Scholl, D. / Sigoillot, M. / Overtus, M. / Martinez, R.C. / Martens, C. / Wang, Y. / Pardon, E. / Laeremans, T. / Garcia-Pino, A. / Steyaert, J. / Sheppard, D.N. / Hendrix, J. / Govaerts, C.
External linksNat. Chem. Biol. / PubMed:34341587
MethodsX-ray diffraction
Resolution2.705 Å
Structure data

PDB-6ze1:
human NBD1 of CFTR in complex with nanobody G11a
Method: X-RAY DIFFRACTION / Resolution: 2.705 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • lama glama (llama)
KeywordsHYDROLASE / cystic fibrosis / CFTR / nanobodies / allostery / conformational change

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