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

János Almássy, P. Nánási

Research output: Contribution to journalReview article

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.

Original languageEnglish
Pages (from-to)498-502
Number of pages5
JournalCanadian journal of physiology and pharmacology
Volume97
Issue number6
DOIs
Publication statusPublished - Jan 1 2019

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Large-Conductance Calcium-Activated Potassium Channels
Quaternary Protein Structure
Cryoelectron Microscopy
Voltage-Gated Potassium Channels
Mutagenesis
Ligands

Keywords

  • BK channel
  • Horrigan-Aldrich model
  • KCa1.1
  • MaxiK
  • Review
  • Slo1
  • Structure

ASJC Scopus subject areas

  • Physiology
  • Pharmacology
  • Physiology (medical)

Cite this

Brief structural insight into the allosteric gating mechanism of BK (Slo1) channel. / Almássy, János; Nánási, P.

In: Canadian journal of physiology and pharmacology, Vol. 97, No. 6, 01.01.2019, p. 498-502.

Research output: Contribution to journalReview article

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