The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly.

@article{Maraver2003TheOD,
  title={The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly.},
  author={Antonio Maraver and Ana Lucia O{\~n}a O{\~n}a and Fernando Abaitua and Dolores I. Gonz{\'a}lez and Roberto Clemente and Jose A Ruiz-D{\'i}az and Jos{\'e} R Cast{\'o}n and Florencio Pazos and Jos{\'e} Francisco Rodr{\'i}guez},
  journal={Journal of virology},
  year={2003},
  volume={77 11},
  pages={
          6438-49
        }
}
Infectious bursal disease virus (IBDV) capsids are formed by a single protein layer containing three polypeptides, pVP2, VP2, and VP3. Here, we show that the VP3 protein synthesized in insect cells, either after expression of the complete polyprotein or from a VP3 gene construct, is proteolytically degraded, leading to the accumulation of product lacking the 13 C-terminal residues. This finding led to identification of the VP3 oligomerization domain within a 24-amino-acid stretch near the C… CONTINUE READING

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