Abstract
The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0Å 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 β-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. Crown
| Original language | English |
|---|---|
| Pages (from-to) | 1343-1357 |
| Number of pages | 15 |
| Journal | Journal of Molecular Biology |
| Volume | 335 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 30 Jan 2004 |
Keywords
- Haemagglutinin-neuraminidase
- Parainfluenza
- Paramyxovirus
- Protein structure
- Sialic acid
Cite this
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Structure of the Haemagglutinin-neuraminidase from Human Parainfluenza Virus Type III. / Lawrence, Michael C.; Borg, Natalie A.; Streltsov, Victor A.; Pilling, Patricia A.; Epa, V. Chandana; Varghese, Joseph N.; McKimm-Breschkin, Jennifer L.; Colman, Peter M.
In: Journal of Molecular Biology, Vol. 335, No. 5, 30.01.2004, p. 1343-1357.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Structure of the Haemagglutinin-neuraminidase from Human Parainfluenza Virus Type III
AU - Lawrence, Michael C.
AU - Borg, Natalie A.
AU - Streltsov, Victor A.
AU - Pilling, Patricia A.
AU - Epa, V. Chandana
AU - Varghese, Joseph N.
AU - McKimm-Breschkin, Jennifer L.
AU - Colman, Peter M.
PY - 2004/1/30
Y1 - 2004/1/30
N2 - The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0Å 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 β-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. Crown
AB - The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0Å 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 β-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. Crown
KW - Haemagglutinin-neuraminidase
KW - Parainfluenza
KW - Paramyxovirus
KW - Protein structure
KW - Sialic acid
UR - http://www.scopus.com/inward/record.url?scp=0346654073&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2003.11.032
DO - 10.1016/j.jmb.2003.11.032
M3 - Article
C2 - 14729348
AN - SCOPUS:0346654073
VL - 335
SP - 1343
EP - 1357
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 5
ER -