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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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[[Image:2b9b.gif|left|200px]]<br /><applet load="2b9b" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2b9b, resolution 2.85&Aring;" />
caption="2b9b, resolution 2.85&Aring;" />
'''Structure of the Parainfluenza Virus 5 F Protein in its Metastable, Pre-fusion Conformation'''<br />
'''Structure of the Parainfluenza Virus 5 F Protein in its Metastable, Pre-fusion Conformation'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2B9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B9B OCA].
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2B9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B9B OCA].
==Reference==
==Reference==
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[[Category: Simian virus 40]]
[[Category: Simian virus 40]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Jardetzky, T.S.]]
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[[Category: Jardetzky, T S.]]
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[[Category: Lamb, R.A.]]
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[[Category: Lamb, R A.]]
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[[Category: Paterson, R.G.]]
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[[Category: Paterson, R G.]]
[[Category: Wen, X.]]
[[Category: Wen, X.]]
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[[Category: Yin, H.S.]]
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[[Category: Yin, H S.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: fusion protein]]
[[Category: fusion protein]]
[[Category: pre-fusion conformation]]
[[Category: pre-fusion conformation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:39:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:26 2008''

Revision as of 14:35, 21 February 2008


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 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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