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2b9b

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(New page: 200px<br /><applet load="2b9b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b9b, resolution 2.85&Aring;" /> '''Structure of the Par...)
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Revision as of 06:31, 21 November 2007


2b9b, resolution 2.85Å

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Structure of the Parainfluenza Virus 5 F Protein in its Metastable, Pre-fusion Conformation

Overview

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.

About this Structure

2B9B is a Single protein structure of sequence from Simian virus 40 with NAG as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation., Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS, Nature. 2006 Jan 5;439(7072):38-44. PMID:16397490

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