The recognition fragment of the ICP27 peptide is shown docked to the binding pocket on the REF RRM, with selected residues labeled. A similar binding surface on REF/Aly is occupied by an adaptor protein from a different herpesvirus, HVS ORF57. The importance of the key amino acid residues within the binding sites of both viral proteins was confirmed by site-directed mutagenesis. Together, these data precisely map amino acid residues responsible for the direct interactions between viral adaptors and cellular REF/Aly and provide the first molecular details of how herpes viruses access the cellular mRNA export pathway (see Tunnicliffe et al., doi:10.1371/journal.ppat.1001244).
Image Credit: Richard B. Tunnicliffe and Alexander P. Golovanov, University of Manchester
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