A subviral particle binding domain on the rotavirus nonstructural glycoprotein NS28.

@article{Au1993ASP,
  title={A subviral particle binding domain on the rotavirus nonstructural glycoprotein NS28.},
  author={K S Au and Nora Marta Mattion and Mary K. Estes},
  journal={Virology},
  year={1993},
  volume={194 2},
  pages={665-73}
}
The single-shelled particle binding domain(s) on NS28 was examined by testing the ability of different truncated forms of NS28 to bind single-shelled particles (ssp). Deletion of amino acids (aa) 161 to 175 of NS28 abolished ssp binding activity. Deletion of the last three aa (173-175) of NS28 diminished, but did not abolish, the ligand binding activity in our assay conditions. An internal deletion of NS28 (aa 110 to 155) also significantly diminished ssp binding activity in standard binding… CONTINUE READING

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