The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies.Proceedings of the National Academy of Sciences, USA (2005)
AbstractAlthough 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.
- virion protein,
- x-ray structure
Publication DateMarch 10, 2005
Citation InformationHua-Poo Su, Scott Garman, Timothy J. Allison, Christiana Fogg, et al.. "The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies." Proceedings of the National Academy of Sciences, USA Vol. 102 Iss. 12 (2005)
Available at: http://works.bepress.com/scott_garman/1/