Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator.

@article{Regier1993PatternOA,
  title={Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator.},
  author={J L Regier and F Shen and Steven J. Triezenberg},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1993},
  volume={90 3},
  pages={883-7}
}
Structural features of the transcriptional activation domain of the herpes simplex virion protein VP16 were examined by oligonucleotide-directed mutagenesis. Extensive mutagenesis at position 442 of the truncated VP16 activation domain (delta 456), normally occupied by a phenylalanine residue, demonstrated the importance of an aromatic amino acid at that position. On the basis of an alignment of the VP16 sequence surrounding Phe-442 and the sequences of other transcriptional activation domains… CONTINUE READING
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