1ypy

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Revision as of 07:51, 21 November 2007 by OCA (talk | contribs) (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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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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