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. Author manuscript; available in PMC: 2010 Feb 5.
Published in final edited form as: Virology. 2008 Dec 6;384(1):144–150. doi: 10.1016/j.virol.2008.11.016

Figure 5.

Figure 5

Model for gpO action. The “L” shapes represent the gpN monomers. In the full-length gpO protein (A), the N-terminal protease domain (bullet shape) binds (as an oligomer) to the underside of gpN, while interactions between the α-helical domain (cylinders) and between Cys 284 and gpN lead to oligomerization and capsid assembly. In the absence of the N-terminal domain (B), O(195–284) is sufficient to promote correct assembly. O(26–194), however, lacks the required C-terminal domain, and assembly fails (C). The removal of only the C-terminal Cys 284 affects the fidelity of assembly and the size distribution of the procapsids (D). In this case, however, interactions between the α-helical domains can still occur, and about 55% of the shells formed are isometric.