Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1
Structural highlights
1no7 is a 2 chain structure with sequence from Human alphaherpesvirus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
MCP_HHV11 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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Newcomb WW, Trus BL, Booy FP, Steven AC, Wall JS, Brown JC. Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes. J Mol Biol. 1993 Jul 20;232(2):499-511. PMID:8393939 doi:http://dx.doi.org/10.1006/jmbi.1993.1406
