Normal mode dynamics of voltage-gated K+ channels: gating principle, opening mechanism, and inhibition

Moshe M. Greenberger, Abraham O. Samson

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Voltage-dependent potassium channels open in response to changes in membrane potential and become partially inactivated upon binding of inhibitors. Here we calculate normal mode motion of two voltage-dependent K+ channels, KvAP and Shaker, and their complexes with inhibitors and address the gating principle, opening mechanism, and inhibition. The normal modes indicate that pore expansion and channel opening is correlated with a displacement of the arginine gating charges and a tilting of the voltage-sensor paddles. Normal modes of Shaker in complex with agitoxin, which blocks the central pore, do not display significantly altered paddle tilting and pore expansion. In contrast, normal modes of Shaker in complex with hanatoxin, which binds to the voltage sensor paddle, display decreased paddle tilting and pore expansion. This study presents a unified motion for the gating principle and channel opening, and offers insight into the voltage sensor paddle motion and its inhibition.

Original languageEnglish
Pages (from-to)83-88
Number of pages6
JournalJournal of Computational Neuroscience
Volume38
Issue number1
DOIs
StatePublished - Feb 2015

Bibliographical note

Publisher Copyright:
© 2014, Springer Science+Business Media New York.

Keywords

  • Agitoxin
  • Elastic network
  • Gating charges
  • Hanatoxin
  • Molecular dynamics
  • Normal modes
  • Voltage-dependent K channels
  • Voltage-sensor paddle

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