The M2 proton channel from influenza A virus forms proton-selective ion channels, which are the target of the drug amantadine. Here, existing experimental data are quantitatively examined for insights into mechanisms to account for the pH- and voltage-dependences of M2 proton conduction. The analysis shows that a model involving protonation equilibria of His37, including pH-dependent changes in the relative rates of diffusion on either side of the pore, is quantitatively able to account for recently reported electrophysiological data examining the pH- and voltage-dependences of Rostock and Weybridge strain M2 proton conduction.
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The M2 proton channel from influenza A virus forms proton-selective ion channels, which are the target of the drug amantadine. Here, existing experimental data are quantitatively examined for insights into mechanisms to account for the pH- and voltage-dependences of M2 proton conduction. The analysis shows that a model involving protonation equilibria of His37, including pH-dependent changes in the relative rates of diffusion on either side of the pore, is quantitatively able to account for recently reported electrophysiological data examining the pH- and voltage-dependences of Rostock and Weybridge strain M2 proton conduction.
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| uniprot:name |
FEBS Lett.
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| uniprot:author |
Lear J.D.
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| uniprot:date |
2003
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| uniprot:pages |
17-22
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| uniprot:title |
Proton conduction through the M2 protein of the influenza A virus; a quantitative, mechanistic analysis of experimental data.
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| uniprot:volume |
552
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| dc-term:identifier |
doi:10.1016/S0014-5793(03)00778-6
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