Exposing the flexibility of human parainfluenza virus hemagglutinin- neuraminidase

Winger, Moritz and von Itzstein, Mark (2012) Exposing the flexibility of human parainfluenza virus hemagglutinin- neuraminidase. Journal of the American Chemical Society, 134 44: 18447-18452. doi:10.1021/ja3084658

Author Winger, Moritz
von Itzstein, Mark
Title Exposing the flexibility of human parainfluenza virus hemagglutinin- neuraminidase
Journal name Journal of the American Chemical Society   Check publisher's open access policy
ISSN 0002-7863
Publication date 2012-11-01
Sub-type Article (original research)
DOI 10.1021/ja3084658
Open Access Status
Volume 134
Issue 44
Start page 18447
End page 18452
Total pages 6
Place of publication Washington, DC, United States
Publisher American Chemical Society
Language eng
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 hemagglutinin-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 dynamics 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 antiparainfluenza virus drug discovery.
Keyword Hn-Receptor interaction
2-Deoxy-2,3-Didehydro-N-Acetylneuraminic Acid
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 9 times in Thomson Reuters Web of Science Article | Citations
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