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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 : 002004

Three-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 :

RBID : ISTEX:018FEE2B3B0E1D5A85D593939764493BF7DFFD42

English descriptors

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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Le document en format XML

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<term>Sulphated ester</term>
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<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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