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

Abstract:

: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.

authors

Murti KG,Takimoto T,Laver WG,Portner A

doi

10.1073/pnas.90.4.1523

subject

Has Abstract

pub_date

1993-02-15 00:00:00

pages

1523-5

issue

4

eissn

0027-8424

issn

1091-6490

journal_volume

90

pub_type

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