Exposing the flexibility of human parainfluenza virus haemagglutinin-neuraminidase
Author(s)
Winger, Moritz
von Itzstein, Mark
Griffith University Author(s)
Year published
2012
Metadata
Show full item recordAbstract
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 ...
View more >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.
View less >
View more >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.
View less >
Journal Title
Journal of the American Chemical Society
Volume
134
Issue
44
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