1YPY | pdb_00001ypy

The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies.

(2005) Proc Natl Acad Sci U S A 102: 4240-4245

• PubMed: 15761054 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1073/pnas.0501103102
• Primary Citation of Related Structures:  
  1YPY


• 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.

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Organizational Affiliation: 
• Structural Biology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 12441 Parklawn Drive, Rockville, MD 20852, USA.