1ypy: Difference between revisions

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New page: left|200px<br /><applet load="1ypy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ypy, resolution 1.510Å" /> '''Crystal Structure o...
 
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[[Image:1ypy.gif|left|200px]]<br /><applet load="1ypy" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ypy.gif|left|200px]]<br /><applet load="1ypy" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ypy, resolution 1.510&Aring;" />
caption="1ypy, resolution 1.510&Aring;" />
'''Crystal Structure of Vaccinia Virus L1 protein'''<br />
'''Crystal Structure of Vaccinia Virus L1 protein'''<br />


==Overview==
==Overview==
Although eradicated from nature more than two decades ago, the threat of, smallpox has reemerged because of concerns over its use as a biological, weapon. We present the structure of the poxvirus L1 protein, a molecule, that is conserved throughout the poxvirus family and is nearly identical, in vaccinia virus and in variola virus, which causes smallpox. L1 is a, myristoylated envelope protein that is a potent target for neutralizing, antibodies and an important component of current experimental vaccines., The L1 structure reveals a hydrophobic cavity located adjacent to its N, terminus. The cavity would be capable of shielding the myristate moiety, which is essential for virion assembly. The structure of L1 is a step in, the elucidation of molecular mechanisms common to all poxviruses that may, stimulate the design of safer vaccines and new antipoxvirus drugs.
Although eradicated from nature more than two decades ago, the threat of smallpox has reemerged because of concerns over its use as a biological weapon. We present the structure of the poxvirus L1 protein, a molecule that is conserved throughout the poxvirus family and is nearly identical in vaccinia virus and in variola virus, which causes smallpox. L1 is a myristoylated envelope protein that is a potent target for neutralizing antibodies and an important component of current experimental vaccines. The L1 structure reveals a hydrophobic cavity located adjacent to its N terminus. The cavity would be capable of shielding the myristate moiety, which is essential for virion assembly. The structure of L1 is a step in the elucidation of molecular mechanisms common to all poxviruses that may stimulate the design of safer vaccines and new antipoxvirus drugs.


==About this Structure==
==About this Structure==
1YPY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YPY OCA].  
1YPY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YPY OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Vaccinia virus]]
[[Category: Vaccinia virus]]
[[Category: Allison, T.J.]]
[[Category: Allison, T J.]]
[[Category: Fogg, C.]]
[[Category: Fogg, C.]]
[[Category: Garboczi, D.N.]]
[[Category: Garboczi, D N.]]
[[Category: Garman, S.C.]]
[[Category: Garman, S C.]]
[[Category: Moss, B.]]
[[Category: Moss, B.]]
[[Category: Su, H.P.]]
[[Category: Su, H P.]]
[[Category: l1]]
[[Category: l1]]
[[Category: orthopox]]
[[Category: orthopox]]
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[[Category: variola virus]]
[[Category: variola virus]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:53 2008''

Revision as of 17:07, 21 February 2008

File:1ypy.gif


1ypy, resolution 1.510Å

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Crystal Structure of Vaccinia Virus L1 protein

OverviewOverview

Although eradicated from nature more than two decades ago, the threat of smallpox has reemerged because of concerns over its use as a biological weapon. We present the structure of the poxvirus L1 protein, a molecule that is conserved throughout the poxvirus family and is nearly identical in vaccinia virus and in variola virus, which causes smallpox. L1 is a myristoylated envelope protein that is a potent target for neutralizing antibodies and an important component of current experimental vaccines. The L1 structure reveals a hydrophobic cavity located adjacent to its N terminus. The cavity would be capable of shielding the myristate moiety, which is essential for virion assembly. The structure of L1 is a step in the elucidation of molecular mechanisms common to all poxviruses that may stimulate the design of safer vaccines and new antipoxvirus drugs.

About this StructureAbout this Structure

1YPY is a Single protein structure of sequence from Vaccinia virus. Full crystallographic information is available from OCA.

ReferenceReference

The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies., Su HP, Garman SC, Allison TJ, Fogg C, Moss B, Garboczi DN, Proc Natl Acad Sci U S A. 2005 Mar 22;102(12):4240-5. Epub 2005 Mar 10. PMID:15761054

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