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Crystal Structure of Vaccinia Virus L1 proteinCrystal Structure of Vaccinia Virus L1 protein
Structural highlights
Function[L1_VACCW] Envelope protein which probably plays a role in virus entry into the host cell. Is probably involved in the virus attachment to the host cell surface and associates with the entry/fusion complex (EFC). Needed for fusion and penetration of the virus core into host cell.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAlthough 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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