| Literature DB >> 6843658 |
J N Varghese, W G Laver, P M Colman.
Abstract
The influenza virus neuraminidase glycoprotein is a tetramer with a box-shaped head, 100 X 100 X 60 A, attached to a slender stalk. The three-dimensional structure of neuraminidase heads shows that each monomer is composed of six topologically identical beta-sheets arranged in a propeller formation. The tetrameric enzyme has circular 4-fold symmetry stabilized in part by metal ions bound on the symmetry axis. Sugar residues are attached to four of the five potential glycosylation sequences, and in one case contribute to the interaction between subunits in the tetramer.Entities:
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Year: 1983 PMID: 6843658 DOI: 10.1038/303035a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962