Ion channel gating: insights via molecular simulations |
| |
Authors: | Beckstein Oliver Biggin Philip C Bond Peter Bright Joanne N Domene Carmen Grottesi Alessandro Holyoake John Sansom Mark S P |
| |
Institution: | Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. |
| |
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. |
| |
Keywords: | Ion channel Molecolar dynamics Gating Pore Outer membrane protein Nanopore |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|