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Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain.

Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain. Research Abstract Details 

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  • Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain. Abstract Text:

    minyong liMinyong Li,binghe wangBinghe Wang,

    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.

    Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain. Publishing Authors By Initials

    m liM Li,b wangB Wang,

    For similar proteins: viral proteins: viral nonstructural proteins research abstracts see: proteins: viral proteins: viral nonstructural proteins research

    PUBMED ID PMID:

    MEDLINE DATE:

    Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of molecular modeling

    VOLUME: 13

    Page Numbers: 1237-44

    Journal Abbreviation:

    ISSN: 0948-5023

    DAY: 5

    MONTH: 10

    YEAR: 2007

    Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 9806569

    Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain. Keywords Mesh Terms:

    KEYWORDS: Viral Nonstructural Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain. Information

    Substance Name: Protein Kinases

    Registry Number: EC 2.7.1.37

    Grant and Affiliation Information for Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain.

    AFFILIATION: Department of Chemistry and Center for Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30302-4098, USA.

    Country: Germany

    Germany Research PublicationGermany Research Publication

    AGENCY: United States NCI

    GRANT: CA123329

    ACRONYM: CA

    MEDLINETA: J Mol Model

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Homology modeling and examination of the effect of the D92E mutation on the H5N1 nonstructural protein NS1 effector domain Related Publications

     

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