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Title
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Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution.
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Authors
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J.N.Varghese,
P.M.Colman.
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Ref.
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J Mol Biol, 1991,
221,
473-486.
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PubMed id
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Abstract
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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 A resolution. The crystallographic residual is 0.21 for
data between 6 and 2.2 A resolution and the r.m.s. deviations from ideal
geometry are 0.02 A 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 beta-sheet propeller as described
earlier and details of the intramolecular interactions between the six
beta-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.
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