Chloride channels articles within Nature

Featured

• Article
  22 March 2023 | Open Access

  CFTR function, pathology and pharmacology at single-molecule resolution

  A structure–function analysis of cystic fibrosis transmembrane conductance regulator shows its two nucleotide-binding domains dimerize before channel opening, and reveals a mechanism through which conformational changes in the channel regulate chloride conductance.

  • Jesper Levring
  • , Daniel S. Terry
  •  & Jue Chen

• Article | 26 October 2022

  Bestrophin-2 and glutamine synthetase form a complex for glutamate release

  Electrophysiological, structural and biochemical studies on the bestrophin-2 anion channel reveal asymmetric permeability to glutamate and show that it forms a cooperative machinery in complex with glutamine synthetase for glutamate release.

  • Aaron P. Owji
  • , Kuai Yu
  •  & Tingting Yang

• Article | 04 November 2020

  Structures and pH-sensing mechanism of the proton-activated chloride channel

  Cryo-electron microscopy structures of the human proton-activated chloride channel (PAC) shed light on its pH-dependent gating mechanism and anion selectivity.

  • Zheng Ruan
  • , James Osei-Owusu
  •  & Wei Lü

• Article | 16 May 2018

  Structure of a volume-regulated anion channel of the LRRC8 family

  The structure of a homomeric channel of subunit A of leucine-rich repeat-containing protein 8 (LRRC8) determined by cryo-electron microscopy and X-ray crystallography reveals the basis for anion selectivity.

  • Dawid Deneka
  • , Marta Sawicka
  •  & Raimund Dutzler

• Letter | 13 December 2017

  Activation mechanism of the calcium-activated chloride channel TMEM16A revealed by cryo-EM

  Cryo-electron microscopy mapping of the calcium-activated chloride channel TMEM16A combined with functional experiments reveals that calcium ions interact directly with the pore to activate the channel.

  • Cristina Paulino
  • , Valeria Kalienkova
  •  & Raimund Dutzler

• Article | 12 November 2014

  X-ray structure of a calcium-activated TMEM16 lipid scramblase

  The authors describe the structure of a Ca²⁺-activated lipid scramblase which catalyses the passive movement of lipids between the two leaflets of a lipid bilayer; the structure reveals the location of a regulatory calcium-binding site embedded within the membrane and the presence of a hydrophilic membrane-traversing cavity that is exposed to the lipid bilayer, where catalysis is likely to occur.

  • Janine D. Brunner
  • , Novandy K. Lim
  •  & Raimund Dutzler

• Article | 22 October 2014

  Structure and insights into the function of a Ca²⁺-activated Cl⁻ channel

  The X-ray crystal structure of a eukaryotic Ca²⁺-activated chloride channel, BEST1, and its function in liposomes are described; the structure shows that Ca²⁺ binds to the cytosolic region of this pentameric channel and reveals that the pore is approximately 95 Å long with at least 15 distinct anion-binding sites.

  • Veronica Kane Dickson
  • , Leanne Pedi
  •  & Stephen B. Long

• Article | 15 May 2011

  Principles of activation and permeation in an anion-selective Cys-loop receptor

  • Ryan E. Hibbs
  •  & Eric Gouaux