Structural highlights
Function
PG095_VACCW Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.[1]
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 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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schin AM, Diesterbeck US, Moss B. Insights into the Organization of the Poxvirus Multicomponent Entry-Fusion Complex from Proximity Analyses in Living Infected Cells. J Virol. 2021 Jul 26;95(16):e0085221. PMID:34076488 doi:10.1128/JVI.00852-21
- ↑ Su HP, Garman SC, Allison TJ, Fogg C, Moss B, Garboczi DN. The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies. Proc Natl Acad Sci U S A. 2005 Mar 22;102(12):4240-5. Epub 2005 Mar 10. PMID:15761054
