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|1usr, resolution 2.00Å ()|
|Ligands:||, , , ,|
NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-NEURAMINIDASE: EVIDENCE FOR A SECOND SIALIC ACID BINDING SITE AND IMPLICATIONS FOR FUSION
Paramyxoviruses are the leading cause of respiratory disease in children. Several paramyxoviruses possess a surface glycoprotein, the hemagglutinin-neuraminidase (HN), that is involved in attachment to sialic acid receptors, promotion of fusion, and removal of sialic acid from infected cells and progeny virions. Previously we showed that Newcastle disease virus (NDV) HN contained a pliable sialic acid recognition site that could take two states, a binding state and a catalytic state. Here we present evidence for a second sialic acid binding site at the dimer interface of HN and present a model for its involvement in cell fusion. Three different crystal forms of NDV HN now reveal identical tetrameric arrangements of HN monomers, perhaps indicative of the tetramer association found on the viral surface.
Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion., Zaitsev V, von Itzstein M, Groves D, Kiefel M, Takimoto T, Portner A, Taylor G, J Virol. 2004 Apr;78(7):3733-41. PMID:15016893
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Zaitsev V, von Itzstein M, Groves D, Kiefel M, Takimoto T, Portner A, Taylor G. Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion. J Virol. 2004 Apr;78(7):3733-41. PMID:15016893
- Crennell S, Takimoto T, Portner A, Taylor G. Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat Struct Biol. 2000 Nov;7(11):1068-74. PMID:11062565 doi:10.1038/81002
- Takimoto T, Taylor GL, Crennell SJ, Scroggs RA, Portner A. Crystallization of Newcastle disease virus hemagglutinin-neuraminidase glycoprotein. Virology. 2000 Apr 25;270(1):208-14. PMID:10772993 doi:10.1006/viro.2000.0263