Two possible conducting states of the influenza A virus M2 ion channel.
Molecular dynamics simulations have been performed on protonated four-helix bundles based on the 25-residue Duff-Ashley transmembrane sequence of the M2 channel of the influenza A virus. Well-equilibrated tetrameric channels, with one, two and four of the H37 residues protonated, were investigated. The protonated peptide bundles were immersed in the octane portion of a phase-separated water/octane system, which provided a membrane-mimetic environment. The simulations suggest that there could be two conducting states of the M2 channel corresponding to tetramers containing one or two protonated histidines. The more open structure of the doubly protonated state suggests it would have the higher conductance.
Zhong
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Center for Molecular Modeling and Department of Chemistry, University of Pennsylvania, Philadelphia, PA, USA.
Newns
D M
DM
Pattnaik
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Lear
J D
JD
Klein
M L
ML
D000595:Amino Acid Sequence; D003198:Computer Simulation; D006639:Histidine / Q000737:chemistry / Q000502:physiology; D009980:Influenza A virus / Q000737:chemistry; D007473:Ion Channels / Q000737:chemistry* / Q000502:physiology; D007700:Kinetics; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011522:Protons; D014763:Viral Matrix Proteins / Q000737:chemistry*; D000086082:Viroporin Proteins
D006639:Histidine; D007473:Ion Channels; D011522:Protons; D014763:Viral Matrix Proteins; C031540:M-protein, influenza virus; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins