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  • Exposing the flexibility of human parainfluenza virus haemagglutinin-neuraminidase

    Author(s)
    Winger, Moritz
    von Itzstein, Mark
    Griffith University Author(s)
    von Itzstein, Mark
    Year published
    2012
    Metadata
    Show full item record
    Abstract
    Human parainfluenza virus type 3 (hPIV-3) is a clinically-significant pathogen and is the causative agent of pneumonia and bronchiolitis in children. In this study the solution dynamics of human parainfluenza type 3 haemagglutinin-neuraminidase (HN) have been investigated. A flexible loop around Asp216 that adopts an open conformation in direct vicinity of the active site of the apo-form of the protein and closes upon inhibitor binding has been identified. To date, no available X-ray crystal structure has shown the molecular dynamic simulation-derived predominant loop-conformation states found in the present study. The ...
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    Human parainfluenza virus type 3 (hPIV-3) is a clinically-significant pathogen and is the causative agent of pneumonia and bronchiolitis in children. In this study the solution dynamics of human parainfluenza type 3 haemagglutinin-neuraminidase (HN) have been investigated. A flexible loop around Asp216 that adopts an open conformation in direct vicinity of the active site of the apo-form of the protein and closes upon inhibitor binding has been identified. To date, no available X-ray crystal structure has shown the molecular dynamic simulation-derived predominant loop-conformation states found in the present study. The outcomes of this study provide additional insight into the dynamical properties of hPIV-3 HN and may have important implications in defining HN glycan recognition events, receptor specificity and anti-parainfluenza virus drug discovery.
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    Journal Title
    Journal of the American Chemical Society
    Volume
    134
    Issue
    44
    DOI
    https://doi.org/10.1021/ja3084658
    Copyright Statement
    Self-archiving of the author-manuscript version is not yet supported by this journal. Please refer to the journal link for access to the definitive, published version or contact the authors for more information.
    Subject
    Chemical sciences
    Biomolecular modelling and design
    Publication URI
    http://hdl.handle.net/10072/48689
    Collection
    • Journal articles

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