Referenced in: none

Automatically associated channels: ClC4

Title: Ion channel gating: insights via molecular simulations.

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

Journal, date & volume: FEBS Lett., 2003 Nov 27 , 555, 85-90

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/14630324

Abstract
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 A) hydrophobic region can form a functionally closed gate in the channel and can be opened by either a small (approximately 1 A) 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.