Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation.

Abstract:

:Enveloped viruses have evolved complex glycoprotein machinery that drives the fusion of viral and cellular membranes, permitting entry of the viral genome into the cell. For the paramyxoviruses, the fusion (F) protein catalyses this membrane merger and entry step, and it has been postulated that the F protein undergoes complex refolding during this process. Here we report the crystal structure of the parainfluenza virus 5 F protein in its prefusion conformation, stabilized by the addition of a carboxy-terminal trimerization domain. The structure of the F protein shows that there are profound conformational differences between the pre- and postfusion states, involving transformations in secondary and tertiary structure. The positions and structural transitions of key parts of the fusion machinery, including the hydrophobic fusion peptide and two helical heptad repeat regions, clarify the mechanism of membrane fusion mediated by the F protein.

journal_name

Nature

journal_title

Nature

authors

Yin HS,Wen X,Paterson RG,Lamb RA,Jardetzky TS

doi

10.1038/nature04322

keywords:

subject

Has Abstract

pub_date

2006-01-05 00:00:00

pages

38-44

issue

7072

eissn

0028-0836

issn

1476-4687

pii

nature04322

journal_volume

439

pub_type

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