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
Naturejournal_title
Natureauthors
Yin HS,Wen X,Paterson RG,Lamb RA,Jardetzky TSdoi
10.1038/nature04322keywords:
subject
Has Abstractpub_date
2006-01-05 00:00:00pages
38-44issue
7072eissn
0028-0836issn
1476-4687pii
nature04322journal_volume
439pub_type
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