1V3C

Structure of the hemagglutinin-neuraminidase from human parainfluenza virus type III: complex with NEU5AC

Summary for 1V3C

• Entry DOI: 10.2210/pdb1v3c/pdb
• Related: 1V2I 1V3B 1V3D 1V3E
• Descriptor: hemagglutinin-neuraminidase glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: piv3 hn, native+neu5ac, hexagonal, hydrolase
• Biological source: Human parainfluenza virus 3
• Total number of polymer chains: 2
• Total formula weight: 98810.80

Authors

Lawrence, M.C.,Borg, N.A.,Streltsov, V.A.,Pilling, P.A.,Epa, V.C.,Varghese, J.N.,McKimm-Breschkin, J.L.,Colman, P.M. (deposition date: 2003-10-30, release date: 2004-02-03, Last modification date: 2024-10-09)

Primary citation

Lawrence, M.C.,Borg, N.A.,Streltsov, V.A.,Pilling, P.A.,Epa, V.C.,Varghese, J.N.,McKimm-Breschkin, J.L.,Colman, P.M.
Structure of the Haemagglutinin-neuraminidase from Human Parainfluenza Virus Type III
J.Mol.Biol., 335:1343-1357, 2004

PubMed Abstract: The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0 A 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 beta-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.

PubMed: 14729348
DOI: 10.1016/j.jmb.2003.11.032

Experimental method

X-RAY DIFFRACTION (2.3 Å)