Evidence that the C-terminal PB2-binding region of the influenza A virus PB1 protein is a discrete alpha-helical domain.

@article{Poole2007EvidenceTT,
  title={Evidence that the C-terminal PB2-binding region of the influenza A virus PB1 protein is a discrete alpha-helical domain.},
  author={Emma L. Poole and Liz Medcalf and Debra Elton and Paul Digard},
  journal={FEBS letters},
  year={2007},
  volume={581 27},
  pages={5300-6}
}
The influenza A virus RNA-dependent RNA polymerase is a heterotrimer composed of PB1, PB2 and PA subunits and essential for viral replication. However, little detailed structural information is available for this important enzyme. We show by circular dichroism spectroscopy that polypeptides from the C-terminus of PB1 that are capable of binding efficiently to PB2 fold into stable alpha-helical structures. Structure prediction analysis of this region of PB1 indicates that it likely consists of a… CONTINUE READING
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