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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Crystals of hemagglutinin-neuraminidase of parainfluenza virus contain triple-stranded helices.

When purified dimers of hemagglutinin-neuraminidase molecules released by protease digestion from three strains of human parainfluenza virus 1 were used in crystallization trials, long thin needle crystals formed. Electron microscopic analysis of these needle crystals revealed that they are composed of stacks of triple-stranded helices with each strand of the helix made up of subunits of hemagglutinin-neuraminidase. To our knowledge, this is the first direct demonstration of the assembly of protein subunits into large triple-stranded helices. An understanding of the organization of these triple helices may shed light on the structural properties of the hemagglutinin-neuraminidase molecules that cause them to form these helices.[1]


  1. Crystals of hemagglutinin-neuraminidase of parainfluenza virus contain triple-stranded helices. Murti, K.G., Takimoto, T., Laver, W.G., Portner, A. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
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