Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
