Role of aromatic localization in the gating process of a potassium channel.

Position of the transmembrane aromatic residues of the KirBac1.1 potassium channel shifts from an even distribution in the closed state toward the membrane/solute interface in the open state model. This is the first example of an integral membrane protein making use of the observed preference for tr...

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Váldodahkkit: Domene, C, Vemparala, S, Klein, M, Vénien-Bryan, C, Doyle, D
Materiálatiipa: Journal article
Giella:English
Almmustuhtton: 2006
Fáttát:
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author Domene, C
Vemparala, S
Klein, M
Vénien-Bryan, C
Doyle, D
author_facet Domene, C
Vemparala, S
Klein, M
Vénien-Bryan, C
Doyle, D
author_sort Domene, C
collection OXFORD
description Position of the transmembrane aromatic residues of the KirBac1.1 potassium channel shifts from an even distribution in the closed state toward the membrane/solute interface in the open state model. This is the first example of an integral membrane protein making use of the observed preference for transmembrane aromatic residues to reside at the interfaces. The process of aromatic localization is proposed as a means of directing and stabilizing structural changes during conformational transitions within the transmembrane region of integral membrane proteins. All-atom molecular dynamics simulations of the open and closed conformers in a membrane environment have been carried out to take account of the interactions between the aromatic residues and the lipids, which may be involved in the conformational change, e.g., the gating of the channel.
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spelling oxford-uuid:341862fc-5c14-4774-8758-1dee584858bf2022-03-26T13:23:48ZRole of aromatic localization in the gating process of a potassium channel.Journal articlehttp://purl.org/coar/resource_type/c_545buuid:341862fc-5c14-4774-8758-1dee584858bfmethodsMolecular ConformationTyrosineG Protein-Coupled Inwardly-Rectifying Potassium ChannelsCell MembraneBiophysicsLipid BilayersIon Channel GatingLipidsComputer SimulationmetabolismPotassium ChannelsTime FactorsModels, MolecularchemistryPhenylalanineEnglishStructural Genomics Consortium2006Domene, CVemparala, SKlein, MVénien-Bryan, CDoyle, DPosition of the transmembrane aromatic residues of the KirBac1.1 potassium channel shifts from an even distribution in the closed state toward the membrane/solute interface in the open state model. This is the first example of an integral membrane protein making use of the observed preference for transmembrane aromatic residues to reside at the interfaces. The process of aromatic localization is proposed as a means of directing and stabilizing structural changes during conformational transitions within the transmembrane region of integral membrane proteins. All-atom molecular dynamics simulations of the open and closed conformers in a membrane environment have been carried out to take account of the interactions between the aromatic residues and the lipids, which may be involved in the conformational change, e.g., the gating of the channel.
spellingShingle methods
Molecular Conformation
Tyrosine
G Protein-Coupled Inwardly-Rectifying Potassium Channels
Cell Membrane
Biophysics
Lipid Bilayers
Ion Channel Gating
Lipids
Computer Simulation
metabolism
Potassium Channels
Time Factors
Models, Molecular
chemistry
Phenylalanine
Domene, C
Vemparala, S
Klein, M
Vénien-Bryan, C
Doyle, D
Role of aromatic localization in the gating process of a potassium channel.
title Role of aromatic localization in the gating process of a potassium channel.
title_full Role of aromatic localization in the gating process of a potassium channel.
title_fullStr Role of aromatic localization in the gating process of a potassium channel.
title_full_unstemmed Role of aromatic localization in the gating process of a potassium channel.
title_short Role of aromatic localization in the gating process of a potassium channel.
title_sort role of aromatic localization in the gating process of a potassium channel
topic methods
Molecular Conformation
Tyrosine
G Protein-Coupled Inwardly-Rectifying Potassium Channels
Cell Membrane
Biophysics
Lipid Bilayers
Ion Channel Gating
Lipids
Computer Simulation
metabolism
Potassium Channels
Time Factors
Models, Molecular
chemistry
Phenylalanine
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