1YPY

Crystal Structure of Vaccinia Virus L1 protein

Summary for 1YPY

• Entry DOI: 10.2210/pdb1ypy/pdb
• Descriptor: Virion membrane protein (2 entities in total)
• Functional Keywords: vaccinia virus, orthopox, variola virus, smallpox, l1, viral protein
• Biological source: Vaccinia virus
• Cellular location: Virion membrane ; Single-pass membrane protein : P07612
• Total number of polymer chains: 2
• Total formula weight: 39065.75

Authors

Su, H.P.,Garman, S.C.,Allison, T.J.,Fogg, C.,Moss, B.,Garboczi, D.N. (deposition date: 2005-01-31, release date: 2005-03-01, Last modification date: 2024-10-09)

Primary citation

Su, H.P.,Garman, S.C.,Allison, T.J.,Fogg, C.,Moss, B.,Garboczi, D.N.
The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies.
Proc.Natl.Acad.Sci.Usa, 102:4240-4245, 2005

PubMed Abstract: 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.

PubMed: 15761054
DOI: 10.1073/pnas.0501103102

Experimental method

X-RAY DIFFRACTION (1.51 Å)