Selectivity and permeation of alkali metal ions in K +-channels

Ion conduction in K +-channels is usually described in terms of concerted movements of K + progressing in a single file through a narrow pore. Permeation is driven by an incoming ion knocking on those ions already inside the protein. A fine-tuned balan...

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Main Authors: Furini, S, Domene, C
Format: Journal article
Language:English
Published: 2011
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author Furini, S
Domene, C
author_facet Furini, S
Domene, C
author_sort Furini, S
collection OXFORD
description Ion conduction in K +-channels is usually described in terms of concerted movements of K + progressing in a single file through a narrow pore. Permeation is driven by an incoming ion knocking on those ions already inside the protein. A fine-tuned balance between high-affinity binding and electrostatic repulsive forces between permeant ions is needed to achieve efficient conduction. While K +-channels are known to be highly selective for K + over Na +, some K + channels conduct Na + in the absence of K +. Other ions are known to permeate K +-channels with a more moderate preference and unusual conduction features. We describe an extensive computational study on ion conduction in K +-channels rendering free energy profiles for the translocation of three different alkali ions and some of their mixtures. The free energy maps for Rb + translocation show at atomic level why experimental Rb + conductance is slightly lower than that of K +. In contrast to K + or Rb +, external Na + block K + currents, and the sites where Na + transport is hindered are characterized. Translocation of K +/Na + mixtures is energetically unfavorable owing to the absence of equally spaced ion-binding sites for Na +, excluding Na + from a channel already loaded with K +. © 2011 Elsevier Ltd. All rights reserved.
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spelling oxford-uuid:0896e38c-f59f-446f-b952-743f8e6898672022-03-26T09:13:39ZSelectivity and permeation of alkali metal ions in K +-channelsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:0896e38c-f59f-446f-b952-743f8e689867EnglishSymplectic Elements at Oxford2011Furini, SDomene, CIon conduction in K +-channels is usually described in terms of concerted movements of K + progressing in a single file through a narrow pore. Permeation is driven by an incoming ion knocking on those ions already inside the protein. A fine-tuned balance between high-affinity binding and electrostatic repulsive forces between permeant ions is needed to achieve efficient conduction. While K +-channels are known to be highly selective for K + over Na +, some K + channels conduct Na + in the absence of K +. Other ions are known to permeate K +-channels with a more moderate preference and unusual conduction features. We describe an extensive computational study on ion conduction in K +-channels rendering free energy profiles for the translocation of three different alkali ions and some of their mixtures. The free energy maps for Rb + translocation show at atomic level why experimental Rb + conductance is slightly lower than that of K +. In contrast to K + or Rb +, external Na + block K + currents, and the sites where Na + transport is hindered are characterized. Translocation of K +/Na + mixtures is energetically unfavorable owing to the absence of equally spaced ion-binding sites for Na +, excluding Na + from a channel already loaded with K +. © 2011 Elsevier Ltd. All rights reserved.
spellingShingle Furini, S
Domene, C
Selectivity and permeation of alkali metal ions in K +-channels
title Selectivity and permeation of alkali metal ions in K +-channels
title_full Selectivity and permeation of alkali metal ions in K +-channels
title_fullStr Selectivity and permeation of alkali metal ions in K +-channels
title_full_unstemmed Selectivity and permeation of alkali metal ions in K +-channels
title_short Selectivity and permeation of alkali metal ions in K +-channels
title_sort selectivity and permeation of alkali metal ions in k channels
work_keys_str_mv AT furinis selectivityandpermeationofalkalimetalionsinkchannels
AT domenec selectivityandpermeationofalkalimetalionsinkchannels