Varghese J N, Laver W G, Colman P M
Nature. 1983;303(5912):35-40. doi: 10.1038/303035a0.
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.
流感病毒神经氨酸酶糖蛋白是一种四聚体，其头部呈盒状，尺寸为100×100×60埃，连接着一条细长的柄。神经氨酸酶头部的三维结构表明，每个单体由六个拓扑结构相同的β折叠片组成，呈螺旋桨状排列。四聚体酶具有圆形四重对称性，部分通过结合在对称轴上的金属离子得以稳定。糖基连接到五个潜在糖基化序列中的四个上，在一种情况下，有助于四聚体中亚基之间的相互作用。
