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Ion channel gating: insights via molecular simulations
Author(s) -
Beckstein Oliver,
Biggin Philip C,
Bond Peter,
Bright Joanne N,
Domene Carmen,
Grottesi Alessandro,
Holyoake John,
Sansom Mark S.P
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01151-7
Subject(s) - gating , molecular dynamics , kcsa potassium channel , nanopore , ion channel , biophysics , chemical physics , chemistry , membrane , polarity (international relations) , electrostatics , radius , channel (broadcasting) , ion , crystallography , materials science , nanotechnology , computational chemistry , computer science , biochemistry , computer network , receptor , computer security , organic chemistry , cell , biology
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.