Histidine protonation and the activation of viral fusion proteins.

@article{Mueller2008HistidinePA,
  title={Histidine protonation and the activation of viral fusion proteins.},
  author={Daniela S Mueller and Thorsten Kampmann and Ragothaman Yennamalli and Paul R. Young and Bostjan Kobe and Alan E. Mark},
  journal={Biochemical Society transactions},
  year={2008},
  volume={36 Pt 1},
  pages={
          43-5
        }
}
Many viral fusion proteins only become activated under mildly acidic condition (pH 4.5-6.5) close to the pK(a) of histidine side-chain protonation. Analysis of the sequences and structures of influenza HA (haemagglutinin) and flaviviral envelope glycoproteins has led to the identification of a number of histidine residues that are not only fully conserved themselves but have local environments that are also highly conserved [Kampmann, Mueller, Mark, Young and Kobe (2006) Structure 14, 1481-1487… CONTINUE READING
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