1USX

Crystal structure of the Newcastle disease virus hemagglutinin-neuraminidase complexed with thiosialoside

Summary for 1USX

• Entry DOI: 10.2210/pdb1usx/pdb
• Related: 1E8T 1E8U 1E8V 1USR
• Descriptor: HEMAGGLUTININ-NEURAMINIDASE GLYCOPROTEIN, N-acetyl-alpha-neuraminic acid-(2-6)-methyl 6-thio-beta-D-galactopyranoside, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID (3 entities in total)
• Functional Keywords: hydrolase, neuraminidase, hemagglutinin, sialidase
• Biological source: NEWCASTLE DISEASE VIRUS
• Total number of polymer chains: 3
• Total formula weight: 151949.00

Authors

Zaitsev, V.,Itzstein, M.,Groves, D.,Kiefel, M.,Takimoto, T.,Portner, A.,Taylor, G. (deposition date: 2003-12-01, release date: 2004-03-19, Last modification date: 2024-11-06)

Primary citation

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., 78:3733-, 2004

PubMed Abstract: 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.

PubMed: 15016893
DOI: 10.1128/JVI.78.7.3733-3741.2004

Experimental method

X-RAY DIFFRACTION (2.7 Å)