Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state.

@article{Russell2004ConservedGR,
  title={Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state.},
  author={Charles J Russell and Theodore S. Jardetzky and Robert A. Lamb},
  journal={Journal of virology},
  year={2004},
  volume={78 24},
  pages={13727-42}
}
Hydrophobic fusion peptides (FPs) are the most highly conserved regions of class I viral fusion-mediating glycoproteins (vFGPs). FPs often contain conserved glycine residues thought to be critical for forming structures that destabilize target membranes. Unexpectedly, a mutation of glycine residues in the FP of the fusion (F) protein from the paramyxovirus simian parainfluenza virus 5 (SV5) resulted in mutant F proteins with hyperactive fusion phenotypes (C. M. Horvath and R. A. Lamb, J. Virol… CONTINUE READING
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