Details

Autor(en) / Beteiligte

• Whicher, Jonathan R
• MacKinnon, Roderick

Titel

Structure of the voltage-gated K⁺ channel Eag1 reveals an alternative voltage sensing mechanism

Ist Teil von

• Science (American Association for the Advancement of Science), 2016-08, Vol.353 (6300), p.664-669

Ort / Verlag

United States: The American Association for the Advancement of Science

Erscheinungsjahr

2016

Link zum Volltext

Quelle

American Association for the Advancement of Science

Beschreibungen/Notizen

• Voltage-gated potassium (K(v)) channels are gated by the movement of the transmembrane voltage sensor, which is coupled, through the helical S4-S5 linker, to the potassium pore. We determined the single-particle cryo-electron microscopy structure of mammalian K(v)10.1, or Eag1, bound to the channel inhibitor calmodulin, at 3.78 angstrom resolution. Unlike previous K(v) structures, the S4-S5 linker of Eag1 is a five-residue loop and the transmembrane segments are not domain swapped, which suggest an alternative mechanism of voltage-dependent gating. Additionally, the structure and position of the S4-S5 linker allow calmodulin to bind to the intracellular domains and to close the potassium pore, independent of voltage-sensor position. The structure reveals an alternative gating mechanism for K(v) channels and provides a template to further understand the gating properties of Eag1 and related channels.