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Basic Characteristics of Mutations
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Mutation Site
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D92E |
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Mutation Site Sentence
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Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain. |
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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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NS1 |
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Standardized Encoding Gene
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NS
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Genotype/Subtype
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H5N1 |
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Viral Reference
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NS1-IAHO3;2GX9
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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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- |
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Location
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HongKong |
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Literature Information
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PMID
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17917748
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Title
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Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain
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Author
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Li M,Wang B
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Journal
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Journal of molecular modeling
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Journal Info
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2007 Dec;13(12):1237-44
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Abstract
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Virulent H5N1 strains of influenza virus often harbor a D92E point mutation in the nonstructural protein NS1. This crucial mutation has been correlated with increased virulence and/or cytokine resistance, but the structural implications of such a change are still unclear. Furthermore, NS1 protein could also be a potential target for the development of novel antiviral agents against H5N1 strains. Therefore, a reasonable 3D model of H5N1 NS1 is important for the understanding of the molecular basis of increased virulence and the design of novel antiviral agents. Based on the crystal structure of a non-H5N1 NS1 protein, a model of H5N1 NS1 was developed by homology modeling, molecular mechanics and molecular dynamics simulations. It was found that the D92E mutation could result in weakened interactions of the carboxylate side chain with other phosphorylated residues, thereby activating phosphorylation of NS1.
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Sequence Data
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-
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