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Basic Characteristics of Mutations
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Mutation Site
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S31N |
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Mutation Site Sentence
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In addition, spectra are shown of the amantadine-resistant mutant, S31N, in the presence and absence of amantadine. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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M2 |
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Standardized Encoding Gene
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M
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Genotype/Subtype
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- |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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Influenza A
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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amantadine |
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Location
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- |
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Literature Information
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PMID
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17384070
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Title
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Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus
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Author
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Hu J,Asbury T,Achuthan S,Li C,Bertram R,Quine JR,Fu R,Cross TA
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Journal
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Biophysical journal
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Journal Info
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2007 Jun 15;92(12):4335-43
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Abstract
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Amantadine is known to block the M2 proton channel of the Influenza A virus. Here, we present a structure of the M2 trans-membrane domain blocked with amantadine, built using orientational constraints obtained from solid-state NMR polarization-inversion-spin-exchange-at-the-magic-angle experiments. The data indicates a kink in the monomer between two helical fragments having 20 degrees and 31 degrees tilt angles with respect to the membrane normal. This monomer structure is then used to construct a plausible model of the tetrameric amantadine-blocked M2 trans-membrane channel. The influence of amantadine binding through comparative cross polarization magic-angle spinning spectra was also observed. In addition, spectra are shown of the amantadine-resistant mutant, S31N, in the presence and absence of amantadine.
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Sequence Data
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-
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