N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil.

@article{Chen1999NAC,
  title={N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil.},
  author={Jiansheng Chen and John J. Skehel and Don C. Wiley},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 16},
  pages={
          8967-72
        }
}

• Jiansheng Chen, John J. Skehel, Don C. Wiley
• Published in
  Proceedings of the National Academy of Sciences…
  1999
• DOI:10.1073/pnas.96.16.8967

The structure of a stable recombinant ectodomain of influenza hemagglutinin HA(2) subunit, EHA(2) (23-185), defined by proteolysis studies of the intact bacterial-expressed ectodomain, was determined to 1.9-A resolution by using x-ray crystallography. The structure reveals a domain composed of N- and C-terminal residues that form an N cap terminating both the N-terminal alpha-helix and the central coiled coil. The N cap is formed by a conserved sequence, and part of it is found in the neutral… CONTINUE READING

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