Moscow University Biological Sciences Bulletin

, Volume 68, Issue 1, pp 8–14

Influence of interionic interactions on functional state and blocker binding of voltage-gated potassium channels

  • K. V. Shaitan
  • O. S. Sokolova
  • A. K. Shaitan
  • M. A. Kasimova
  • V. N. Novoseletskii
  • M. P. Kirpichnikov
Article

DOI: 10.3103/S0096392513010057

Cite this article as:
Shaitan, K.V., Sokolova, O.S., Shaitan, A.K. et al. Moscow Univ. Biol.Sci. Bull. (2013) 68: 8. doi:10.3103/S0096392513010057

Abstract

A mechanism of ion conduction of a voltage-gated potassium channel KcsA was investigated in full-atomic approximation at a trajectory length of 100 ns using the Lomonosov supercomputer. Methods of molecular dynamics were employed. A structure of the KcsA channel in the open state obtained by X-ray structure analysis (PDB ID 3fb7) was used. Free energy profiles of the KcsA pore occupied with either one or three potassium ions were calculated. It was shown that, under physiological conditions, ions pass through the channel pore cooperatively and the mechanism most probably includes three ions permeating in concert. Interactions of the mammalian voltage-gated channel Kv1.2 with neurotoxin were investigated. It was demonstrated that the effect of interionic interactions on binding of a blocker is rather insufficient.

Keywords

voltage-gated potassium channelsneurotoxinmolecular dynamicsinterionic interactions

Copyright information

© Allerton Press, Inc. 2013

Authors and Affiliations

  • K. V. Shaitan
    • 1
  • O. S. Sokolova
    • 1
  • A. K. Shaitan
    • 1
  • M. A. Kasimova
    • 1
  • V. N. Novoseletskii
    • 1
  • M. P. Kirpichnikov
    • 1
  1. 1.Department of BiologyMoscow State UniversityMoscowRussia