Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. 2004

Michael C Lawrence, and Natalie A Borg, and Victor A Streltsov, and Patricia A Pilling, and V Chandana Epa, and Joseph N Varghese, and Jennifer L McKimm-Breschkin, and Peter M Colman
CSIRO Health Sciences and Nutrition, 343 Royal Parade, Parkville, Vic 3052, Australia. mike.lawrence@csiro.au

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.

UI MeSH Term Description Entries
D008024 Ligands A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) Ligand
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009522 Newcastle disease virus The most well known avian paramyxovirus in the genus AVULAVIRUS and the cause of a highly infectious pneumoencephalitis in fowl. It is also reported to cause CONJUNCTIVITIS in humans. Transmission is by droplet inhalation or ingestion of contaminated water or food. Avian Paramyxovirus 1,Paramyxovirus 1, Avian
D010224 Parainfluenza Virus 3, Human A species of RESPIROVIRUS frequently isolated from small children with pharyngitis, bronchitis, and pneumonia. Hemadsorption Virus 1,Human parainfluenza virus 3,Para-Influenza Virus Type 3,Parainfluenza Virus Type 3,Para Influenza Virus Type 3
D010253 Respirovirus Infections Infections with viruses of the genus RESPIROVIRUS, family PARAMYXOVIRIDAE. Host cell infection occurs by adsorption, via HEMAGGLUTININ, to the cell surface. Infections, Respirovirus
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011991 Receptors, Virus Specific molecular components of the cell capable of recognizing and interacting with a virus, and which, after binding it, are capable of generating some signal that initiates the chain of events leading to the biological response. Viral Entry Receptor,Viral Entry Receptors,Virus Attachment Factor,Virus Attachment Factors,Virus Attachment Receptor,Virus Attachment Receptors,Virus Entry Receptor,Virus Entry Receptors,Virus Receptor,Virus Receptors,Attachment Factor, Virus,Attachment Factors, Virus,Attachment Receptor, Virus,Attachment Receptors, Virus,Entry Receptor, Viral,Entry Receptor, Virus,Entry Receptors, Viral,Entry Receptors, Virus,Receptor, Viral Entry,Receptor, Virus,Receptor, Virus Attachment,Receptor, Virus Entry,Receptors, Viral Entry,Receptors, Virus Attachment,Receptors, Virus Entry
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D003460 Crystallization The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Crystalline Polymorphs,Polymorphism, Crystallization,Crystal Growth,Polymorphic Crystals,Crystal, Polymorphic,Crystalline Polymorph,Crystallization Polymorphism,Crystallization Polymorphisms,Crystals, Polymorphic,Growth, Crystal,Polymorph, Crystalline,Polymorphic Crystal,Polymorphisms, Crystallization,Polymorphs, Crystalline
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

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