Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III
- Author(s)
- Lawrence, MC; Borg, NA; Streltsov, VA; Pilling, PA; Epa, VC; Varghese, JN; McKimm-Breschkin, JL; Colman, PM;
- Details
- Publication Year 2004-01-30,Volume 335,Issue #5,Page 1343-1357
- Journal Title
- JOURNAL OF MOLECULAR BIOLOGY
- Publication Type
- Journal Article
- Abstract
- The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0 Angstrom resolution, both in native form and in complex with three substrate analogues. In support of earlier work on the structure of the homologous protein from the avian pathogen Newcastle disease virus (NDV), we observe a dimer of beta-propellers and find no evidence for spatially separated sites performing the receptor-binding and neuraminidase functions of the protein. As with the NDV HN, the active site of the HN of parainfluenza viruses is structurally flexible, suggesting that it may be able to switch between a receptor-binding state and a catalytic state. However, in contrast to the NDV structures, we observe no ligand-induced structural changes that extend beyond the active site and modify the dimer interface. Crown Copyright (C) 2003 Published by Elsevier Ltd. All rights reserved.
- Publisher
- ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
- Keywords
- NEWCASTLE-DISEASE VIRUS; AVIAN INFLUENZA-VIRUS; ACID BINDING-SITE; SIALIC-ACID; CRYSTAL-STRUCTURE; 3-DIMENSIONAL STRUCTURE; BACTERIAL SIALIDASE; 4-GU-DANA ZANAMIVIR; STRUCTURE ALIGNMENT; ELECTRON-DENSITY
- Publisher's Version
- https://doi.org/10.1016/j.jmb.2003.11.032
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2004-01-30 12:00:00