1ypy

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|ACTIVITY=
|ACTIVITY=
|GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus])
|GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ypy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ypy OCA], [http://www.ebi.ac.uk/pdbsum/1ypy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ypy RCSB]</span>
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[[Category: variola virus]]
[[Category: variola virus]]
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Revision as of 22:17, 30 March 2008


PDB ID 1ypy

Drag the structure with the mouse to rotate
, resolution 1.510Å
Gene: L1 (Vaccinia virus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Vaccinia Virus L1 protein


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.

About this Structure

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

Reference

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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