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Hydrolase PDB id
Protein chains
448 a.a. *
SIA ×2
DAN ×2
NDG ×2
_CA ×2
Waters ×921
* Residue conservation analysis

References listed in PDB file
Key reference
Title Second sialic acid binding site in newcastle disease virus hemagglutinin-Neuraminidase: implications for fusion.
Authors V.Zaitsev, M.Von itzstein, D.Groves, M.Kiefel, T.Takimoto, A.Portner, G.Taylor.
Ref. J Virol, 2004, 78, 3733-3741.
PubMed id 15016893
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.
Secondary reference #1
Title Crystal structure of the multifunctional paramyxovirus hemagglutinin-Neuraminidase.
Authors S.Crennell, T.Takimoto, A.Portner, G.Taylor.
Ref. Nat Struct Biol, 2000, 7, 1068-1074. [DOI no: 10.1038/81002]
PubMed id 11062565
Full text Abstract
Figure 1.
Figure 1. Schematic representations of the crystal structure of HN. The chains are colored from blue at the N-terminus through to red at the C-terminus. The N-linked carbohydrate residues are shown in ball and stick representation, and the divalent metal ions are drawn as gray spheres. a, The HN dimer observed in the orthorhombic crystal form, viewed down the NCS two-fold axis showing the location of the -anomer of sialic acid drawn as a space filling molecule. b, The dimer of the HN -Neu5Ac2en complex observed in the hexagonal crystal form, viewed down the NCS two-fold axis. c, The image in (b) rotated by 45 around a horizontal axis and colored according to B-factor conveniently reveals orthogonal views of the HN monomer. Coloring is from dark blue (B = 10 2) to deep red (B = 60 2).
Figure 3.
Figure 3. The active site. a, The inhibitor Neu5Ac2en bound in the active site of the hexagonal crystal form. b, The same active site as observed in the ligand-free pH 4.6 orthorhombic crystal structure. c, The -anomer of sialic acid bound in the active site of the pH 4.6 orthorhombic crystal form, showing hydrogen bonding interactions (dotted lines). Water molecules are labeled W.
The above figures are reproduced from the cited reference with permission from Macmillan Publishers Ltd
Secondary reference #2
Title Crystallization of newcastle disease virus hemagglutinin-Neuraminidase glycoprotein.
Authors T.Takimoto, G.L.Taylor, S.J.Crennell, R.A.Scroggs, A.Portner.
Ref. Virology, 2000, 270, 208-214. [DOI no: 10.1006/viro.2000.0263]
PubMed id 10772993
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