1z4y
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Parainfluenza Virus 5 (SV5) Hemagglutinin-Neuraminidase (HN) (pH 8.0)
OverviewOverview
The paramyxovirus hemagglutinin-neuraminidase (HN) functions in virus, attachment to cells, cleavage of sialic acid from oligosaccharides, and, stimulating membrane fusion during virus entry into cells. The structural, basis for these diverse functions remains to be fully understood. We, report the crystal structures of the parainfluenza virus 5 (SV5) HN and, its complexes with sialic acid, the inhibitor DANA, and the receptor, sialyllactose. SV5 HN shares common structural features with HN of, Newcastle disease virus (NDV) and human parainfluenza 3 (HPIV3), but, unlike the previously determined HN structures, the SV5 HN forms a, tetramer in solution, which is thought to be the physiological oligomer., The sialyllactose complex reveals intact receptor within the active site, but no major conformational changes in the protein. The SV5 HN structures, do not support previously proposed models for HN action in membrane fusion, and suggest alternative mechanisms by which HN may promote virus entry, into cells.
About this StructureAbout this Structure
1Z4Y is a Single protein structure of sequence from Simian virus 5 with NDG and CA as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Full crystallographic information is available from OCA.
ReferenceReference
Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose., Yuan P, Thompson TB, Wurzburg BA, Paterson RG, Lamb RA, Jardetzky TS, Structure. 2005 May;13(5):803-15. PMID:15893670
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