Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2·2 Å resolution
Identifieur interne : 002003 ( Main/Exploration ); précédent : 002002; suivant : 002004Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2·2 Å resolution
Auteurs : J. N. Varghese [Australie] ; P. M. Colman [Australie]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1991.
English descriptors
- Teeft :
- Academic press, Acta crystallogr, Active site, Active site neighbouring, Amino acid residues, Amino acid sequence, Antigenic, Asian strain, Asparagine residues, Atomic model, Backbone model, Bond lengths, Bottom surface, Carbohydrate, Carbohydrate chains, Carbohydrate side chains, Chemical analysis, Colman, Colman figure, Conformation, Continuous density, Crystal contact, Data collection, Diffraction data, Disulphide, Disulphide bonds, Disulphide bridge, Early stages, Electron density, Extensive bulge, Extensive loop, First strand, Fourth strand, Glcnac, Glcnac residues, Glycosylation sites, Graphics device, Haemagglutinin, Head regions, Higher temperature factors, Host cells, Human influenza virus, Hydrogen bonds, Hydrophobic core, Hydrophobic interactions, Influenza, Influenza virus, Influenza virus neuraminidase, Influenza viruses, Inner strands, Ionic interactions, Laver, Monomer, Neighbouring, Neighbouring subunit, Neuraminidase, Neuraminidase heads, Neuraminidase structure figure, Oligosaccharide, Outer strand, Peptide, Peptide bonds, Peptide nitrogen, Peptide oxygens, Peptide plane, Plenum publishing corporation, Propeller, Propeller axis, Protein structure, Putative, Putative site, Ramachandran plot, Refined structure, Refinement, Residue, Residue number, Resolution range, Sialic acid, Site neighbouring, Solvent correction, Solvent mask, Solvent molecules, Structure factors, Subtypes, Subunit, Subunit interface, Sugar residues, Sulphated ester, Temperature factor, Tentative carbohydrate chain, Tetramer, Tetrameric heads, Tetramers face, Unpublished results, Upper surface, Varghese, Varghese colman, Viral, Viral membrane, Ward dopheide, Water molecule, Water molecules.
Abstract
Abstract: An atomic model of the tetrameric surface glycoprotein neuraminidase of influenza virus A/Tokyo/3/67 has been built and refined based on X-ray diffraction data at 2·2 Å resolution. The crystallographic residual is 0·21 for data between 6 and 2·2 Å resolution and the r.m.s. deviations from ideal geometry are 0·02 Å for bond lengths and 3·9 degrees for bond angles. The model includes amino acid residues 83 to 469, four oligosaccharide structures N-linked at asparagine residues 86, 146, 200 and 234, a single putative Ca2+ ion site, and 85 water molecules. One of the oligosaccharides participates in a novel crystal contact. The folding pattern is a β-sheet propeller as described earlier and details of the intramolecular interactions between the six β-sheets are presented. Strain-invariant residues are clustered around the propeller axis on the upper surface of the molecule where they line the wall of a cavity into which sialic has been observed to bind. Strain-variable residues implicated in binding to antibodies surround this site.
Url:
DOI: 10.1016/0022-2836(91)80068-6
Affiliations:
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<term>Amino acid sequence</term>
<term>Antigenic</term>
<term>Asian strain</term>
<term>Asparagine residues</term>
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<term>Bond lengths</term>
<term>Bottom surface</term>
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<term>Chemical analysis</term>
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<term>Colman figure</term>
<term>Conformation</term>
<term>Continuous density</term>
<term>Crystal contact</term>
<term>Data collection</term>
<term>Diffraction data</term>
<term>Disulphide</term>
<term>Disulphide bonds</term>
<term>Disulphide bridge</term>
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<term>Electron density</term>
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<term>Glcnac residues</term>
<term>Glycosylation sites</term>
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<term>Haemagglutinin</term>
<term>Head regions</term>
<term>Higher temperature factors</term>
<term>Host cells</term>
<term>Human influenza virus</term>
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<term>Hydrophobic core</term>
<term>Hydrophobic interactions</term>
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<term>Influenza virus</term>
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<term>Ramachandran plot</term>
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<term>Refinement</term>
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<term>Residue number</term>
<term>Resolution range</term>
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<term>Site neighbouring</term>
<term>Solvent correction</term>
<term>Solvent mask</term>
<term>Solvent molecules</term>
<term>Structure factors</term>
<term>Subtypes</term>
<term>Subunit</term>
<term>Subunit interface</term>
<term>Sugar residues</term>
<term>Sulphated ester</term>
<term>Temperature factor</term>
<term>Tentative carbohydrate chain</term>
<term>Tetramer</term>
<term>Tetrameric heads</term>
<term>Tetramers face</term>
<term>Unpublished results</term>
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<term>Varghese</term>
<term>Varghese colman</term>
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<front><div type="abstract" xml:lang="en">Abstract: An atomic model of the tetrameric surface glycoprotein neuraminidase of influenza virus A/Tokyo/3/67 has been built and refined based on X-ray diffraction data at 2·2 Å resolution. The crystallographic residual is 0·21 for data between 6 and 2·2 Å resolution and the r.m.s. deviations from ideal geometry are 0·02 Å for bond lengths and 3·9 degrees for bond angles. The model includes amino acid residues 83 to 469, four oligosaccharide structures N-linked at asparagine residues 86, 146, 200 and 234, a single putative Ca2+ ion site, and 85 water molecules. One of the oligosaccharides participates in a novel crystal contact. The folding pattern is a β-sheet propeller as described earlier and details of the intramolecular interactions between the six β-sheets are presented. Strain-invariant residues are clustered around the propeller axis on the upper surface of the molecule where they line the wall of a cavity into which sialic has been observed to bind. Strain-variable residues implicated in binding to antibodies surround this site.</div>
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