Ion channel gating: insights via molecular simulations

FEBS Letters

Holyoake, John¹  Domene, Carmen¹  Beckstein, Oliver¹  Biggin, Philip C¹  Grottesi, Alessandro¹  Bond, Peter¹  Sansom, Mark S.P¹  Bright, Joanne N¹ 

[1] Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK

关键词: Ion channel;    Molecolar dynamics;    Gating;    Pore;    Outer membrane protein;    Nanopore;   

DOI  :  10.1016/S0014-5793(03)01151-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown