Ion channel gating: Insights via molecular simulations

Oliver Beckstein, Philip C. Biggin, Peter Bond, Joanne N. Bright, Carmen Domene, Alessandro Grottesi, John Holyoake, Mark S.P. Sansom

Research output: Contribution to journalArticlepeer-review

113 Scopus citations


Ion channels are gated, i.e. they can switch conformation between a closed and an open state. Molecular dynamics simulations may be used to study the conformational dynamics of ion channels and of simple channel models. Simulations on model nanopores reveal that a narrow (<4 Å) hydrophobic region can form a functionally closed gate in the channel and can be opened by either a small (∼1 Å) increase in pore radius or an increase in polarity. Modelling and simulation studies confirm the importance of hydrophobic gating in K channels, and support a model in which hinge-bending of the pore-lining M2 (or S6 in Kv channels) helices underlies channel gating. Simulations of a simple outer membrane protein, OmpA, indicate that a gate may also be formed by interactions of charged side chains within a pore, as is also the case in ClC channels.

Original languageEnglish (US)
Pages (from-to)85-90
Number of pages6
JournalFEBS Letters
Issue number1
StatePublished - Nov 27 2003
Externally publishedYes


  • Gating
  • Ion channel
  • Molecolar dynamics
  • Nanopore
  • Outer membrane protein
  • Pore

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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