title: Ion channel gating: insights via molecular simulations.
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.
authors: Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
authors: Oliver
authors: O
authors: Beckstein
authors: Philip C
authors: PC
authors: Biggin
authors: Peter
authors: P
authors: Bond
authors: Joanne N
authors: JN
authors: Bright
authors: Carmen
authors: C
authors: Domene
authors: Alessandro
authors: A
authors: Grottesi
authors: John
authors: J
authors: Holyoake
authors: Mark S P
authors: MS
authors: Sansom
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D015221:Potassium Channels / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D013816:Thermodynamics
chemical_list: D001425:Bacterial Outer Membrane Proteins; D007473:Ion Channels; D015221:Potassium Channels; C078167:OMPA outer membrane proteins