Molecular dynamics simulation approaches to K channels: conformational flexibility and physiological function

Alessandro Grottesi; Carmen Domene Nunez; Shozeb Haider; Mark S. P. Sansom

doi:10.1109/TNB.2004.842473

Molecular dynamics simulation approaches to K channels: conformational flexibility and physiological function

Alessandro Grottesi, Carmen Domene Nunez, Shozeb Haider, Mark S. P. Sansom

Department of Chemistry

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19 Citations (SciVal)

Abstract

Molecular modeling and simulations enable extrapolation for the structure of bacterial potassium channels to the function of their mammalian homologues. Molecular dynamics simulations have revealed the concerted single-file motion of potassium ions and water molecules through the selectivity filter of K channels and the role of filter flexibility in ion permeation and in "fast gating." Principal components analysis of extended K channel simulations suggests that hinge-bending of pore-lining M2 (or S6) helices plays a key role in K channel gating. Based on these and other simulations, a molecular model for gating of inward rectifier K channel gating is presented.

Original language	English
Pages (from-to)	112-120
Number of pages	9
Journal	IEEE TRANSACTIONS ON NANOBIOSCIENCE
Volume	4
Issue number	1
DOIs	https://doi.org/10.1109/TNB.2004.842473
Publication status	Published - 1 Mar 2005

Keywords

Animals, Cell Membrane, Cell Membrane Permeability, Humans, Ion Channel Gating, Kinetics, Membrane Potentials, Models, Biological, Models, Chemical, Motion, Porosity, Potassium Channels, Protein Conformation, Structure-Activity Relationship

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10.1109/TNB.2004.842473

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T1 - Molecular dynamics simulation approaches to K channels: conformational flexibility and physiological function

AU - Grottesi, Alessandro

AU - Domene Nunez, Carmen

AU - Haider, Shozeb

AU - Sansom, Mark S. P.

PY - 2005/3/1

Y1 - 2005/3/1

N2 - Molecular modeling and simulations enable extrapolation for the structure of bacterial potassium channels to the function of their mammalian homologues. Molecular dynamics simulations have revealed the concerted single-file motion of potassium ions and water molecules through the selectivity filter of K channels and the role of filter flexibility in ion permeation and in "fast gating." Principal components analysis of extended K channel simulations suggests that hinge-bending of pore-lining M2 (or S6) helices plays a key role in K channel gating. Based on these and other simulations, a molecular model for gating of inward rectifier K channel gating is presented.

AB - Molecular modeling and simulations enable extrapolation for the structure of bacterial potassium channels to the function of their mammalian homologues. Molecular dynamics simulations have revealed the concerted single-file motion of potassium ions and water molecules through the selectivity filter of K channels and the role of filter flexibility in ion permeation and in "fast gating." Principal components analysis of extended K channel simulations suggests that hinge-bending of pore-lining M2 (or S6) helices plays a key role in K channel gating. Based on these and other simulations, a molecular model for gating of inward rectifier K channel gating is presented.

KW - Animals, Cell Membrane, Cell Membrane Permeability, Humans, Ion Channel Gating, Kinetics, Membrane Potentials, Models, Biological, Models, Chemical, Motion, Porosity, Potassium Channels, Protein Conformation, Structure-Activity Relationship

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DO - 10.1109/TNB.2004.842473

M3 - Article

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JO - IEEE TRANSACTIONS ON NANOBIOSCIENCE

JF - IEEE TRANSACTIONS ON NANOBIOSCIENCE

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Molecular dynamics simulation approaches to K channels: conformational flexibility and physiological function

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