Structural highlights
Function
MCP_EBVB9 Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins.[HAMAP-Rule:MF_04016][1]
References
- ↑ Henson BW, Perkins EM, Cothran JE, Desai P. Self-assembly of Epstein-Barr virus capsids. J Virol. 2009 Apr;83(8):3877-90. Epub 2009 Jan 21. PMID:19158247 doi:http://dx.doi.org/JVI.01733-08
