Structural highlights
Function
Q6WJ03_9MONO Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion.[ARBA:ARBA00025476]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0 A 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.
Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III.,Lawrence MC, Borg NA, Streltsov VA, Pilling PA, Epa VC, Varghese JN, McKimm-Breschkin JL, Colman PM J Mol Biol. 2004 Jan 30;335(5):1343-57. PMID:14729348[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lawrence MC, Borg NA, Streltsov VA, Pilling PA, Epa VC, Varghese JN, McKimm-Breschkin JL, Colman PM. Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. J Mol Biol. 2004 Jan 30;335(5):1343-57. PMID:14729348
