1svb: Difference between revisions

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New page: left|200px<br /><applet load="1svb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1svb, resolution 1.9Å" /> '''ENVELOPE GLYCOPROTEIN...
 
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[[Image:1svb.gif|left|200px]]<br /><applet load="1svb" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1svb.gif|left|200px]]<br /><applet load="1svb" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1svb, resolution 1.9&Aring;" />
caption="1svb, resolution 1.9&Aring;" />
'''ENVELOPE GLYCOPROTEIN FROM TICK-BORNE ENCEPHALITIS VIRUS'''<br />
'''ENVELOPE GLYCOPROTEIN FROM TICK-BORNE ENCEPHALITIS VIRUS'''<br />


==Overview==
==Overview==
The crystallographically determined structure of a soluble fragment from, the major envelope protein of a flavivirus reveals an unusual, architecture. The flat, elongated dimer extends in a direction that would, be parallel to the viral membrane. Residues that influence binding of, monoclonal antibodies lie on the outward-facing surface of the protein., The clustering of mutations that affect virulence in various flaviviruses, indicates a possible receptor binding site and, together with other, mutational and biochemical data, suggests a picture for the, fusion-activating, conformational change triggered by low pH.
The crystallographically determined structure of a soluble fragment from the major envelope protein of a flavivirus reveals an unusual architecture. The flat, elongated dimer extends in a direction that would be parallel to the viral membrane. Residues that influence binding of monoclonal antibodies lie on the outward-facing surface of the protein. The clustering of mutations that affect virulence in various flaviviruses indicates a possible receptor binding site and, together with other mutational and biochemical data, suggests a picture for the fusion-activating, conformational change triggered by low pH.


==About this Structure==
==About this Structure==
1SVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tick-borne_encephalitis_virus Tick-borne encephalitis virus] 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=1SVB OCA].  
1SVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tick-borne_encephalitis_virus Tick-borne encephalitis virus] 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=1SVB OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Tick-borne encephalitis virus]]
[[Category: Tick-borne encephalitis virus]]
[[Category: Harrison, S.C.]]
[[Category: Harrison, S C.]]
[[Category: Rey, F.A.]]
[[Category: Rey, F A.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:32 2008''

Revision as of 13:05, 21 February 2008

File:1svb.gif


1svb, resolution 1.9Å

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ENVELOPE GLYCOPROTEIN FROM TICK-BORNE ENCEPHALITIS VIRUS

Overview

The crystallographically determined structure of a soluble fragment from the major envelope protein of a flavivirus reveals an unusual architecture. The flat, elongated dimer extends in a direction that would be parallel to the viral membrane. Residues that influence binding of monoclonal antibodies lie on the outward-facing surface of the protein. The clustering of mutations that affect virulence in various flaviviruses indicates a possible receptor binding site and, together with other mutational and biochemical data, suggests a picture for the fusion-activating, conformational change triggered by low pH.

About this Structure

1SVB is a Single protein structure of sequence from Tick-borne encephalitis virus with NAG as ligand. Full crystallographic information is available from OCA.

Reference

The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution., Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC, Nature. 1995 May 25;375(6529):291-8. PMID:7753193

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