A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity

The M 2 protein from influenza A virus forms proton-selective channels that are essential to viral function and are the target of the drug amantadine. Cys scanning was used to generate a series of mutants with successive substitutions in the transmembrane segment of the protein, and the mutants were...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1997-10, Vol.94 (21), p.11301-11306
Hauptverfasser:	Pinto, L H, Dieckmann, G R, Gandhi, C S, Papworth, C G, Braman, J, Shaughnessy, M A, Lear, J D, Lamb, R A, DeGrado, W F
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution Animals Biological Sciences Biology Computer Simulation Cysteine Electric Conductivity Female Influenza Influenza A virus - physiology Ion Channels - chemistry Ion Channels - physiology Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mutation Oocytes - physiology Protein Conformation Protein Structure, Secondary Proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism Substrate Specificity Viral Matrix Proteins - chemistry Viral Matrix Proteins - physiology Xenopus laevis
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