Brief structural insight into the allosteric gating mechanism of BK (Slo1) channel 1

Can J Physiol Pharmacol. 2019 Jun;97(6):498-502. doi: 10.1139/cjpp-2018-0516. Epub 2018 Dec 5.

Abstract

The big conductance Ca2+-dependent K+ channel, also known as BK, MaxiK, Slo1, or KCa1.1, is a ligand- and voltage-gated K+ channel. Although structure-function studies of the past decades, involving mutagenesis and electrophysiological measurements, revealed fine details of the mechanism of BK channel gating, the exact molecular details remained unknown until the quaternary structure of the protein has been solved at a resolution of 3.5 Å using cryo-electron microscopy. In this short review, we are going to summarize these results and interpret the gating model of the BK channel in the light of the recent structural results.

Keywords: BK channel; Horrigan–Aldrich model; KCa1.1; MaxiK; Slo1; article de synthèse; canal BK; modèle d’Horrigan–Aldrich; review; structure.

Publication types

  • Review

MeSH terms

  • Allosteric Regulation
  • Animals
  • Humans
  • Ion Channel Gating*
  • Large-Conductance Calcium-Activated Potassium Channels / chemistry*
  • Large-Conductance Calcium-Activated Potassium Channels / metabolism*
  • Models, Molecular

Substances

  • Large-Conductance Calcium-Activated Potassium Channels