Implications of the picornavirus capsid structure for polyprotein processing.

@article{Arnold1987ImplicationsOT,
  title={Implications of the picornavirus capsid structure for polyprotein processing.},
  author={Eddy Arnold and Ming Luo and Gert Vriend and Michael G. Rossmann and Ann C. Palmenberg and Griffith D. Parks and Martin J. H. Nicklin and Eckard J Wimmer},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1987},
  volume={84 1},
  pages={21-5}
}
Mature picornaviral proteins are derived by progressive, posttranslational cleavage of a precursor polyprotein. These cleavages play a role in the control of virus functions. Although the processed termini are separated by as much as 75 A in the native virus capsid, the fold and arrangement of polypeptide chains in a protomer before proteolysis are likely to be similar to that found in the mature virus. The three-dimensional structures of rhinovirus and Mengo virus suggest that the cleavage… CONTINUE READING

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