Structural polymorphism of the major capsid protein of a double-stranded RNA virus: an amphipathic alpha helix as a molecular switch.

@article{Saugar2005StructuralPO,
  title={Structural polymorphism of the major capsid protein of a double-stranded RNA virus: an amphipathic alpha helix as a molecular switch.},
  author={Irene Saugar and Daniel Luque and Ana O{\~n}a and Jos{\'e} Francisco Rodr{\'i}guez and Jos{\'e} L Carrascosa and Benes L Trus and Jos{\'e} R Cast{\'o}n},
  journal={Structure},
  year={2005},
  volume={13 7},
  pages={1007-17}
}
The infectious bursal disease virus T=13 viral particle is composed of two major proteins, VP2 and VP3. Here, we show that the molecular basis of the conformational flexibility of the major capsid protein precursor, pVP2, is an amphipatic alpha helix formed by the sequence GFKDIIRAIR. VP2 containing this alpha helix is able to assemble into the T=13 capsid only when expressed as a chimeric protein with an N-terminal His tag. An amphiphilic alpha helix, which acts as a conformational switch, is… CONTINUE READING