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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

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Chen, Jue, Skehel, John J., Wiley, Don C.·1999·Proceedings of the National Academy of Sciences

Abstract

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-Å 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 α-helix and the central coiled coil. The N cap is formed by a conserved sequence, and part of it is found in the neutral pH conformation of HA. The C-terminal 23 residues of the ectodomain form a 72-Å long nonhelical structure ordered to within 7 residues of the transmembrane anchor. The structure implies that continuous α helices are not required for membrane fusion at either the N or C termini. The difference in stability between recombinant molecules with and without the N cap sequences suggests that additional free energy for membrane fusion may become available after the formation of the central triple-stranded coiled coil and insertion of the fusion peptide into the target membrane.

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Metadata

Authors
Chen, J., Skehel, J. J., & Wiley, D. C.
Venue
Proceedings of the National Academy of Sciences
Published
1999-08-03
Volume
96
Issue
16
Pages
8967-8972
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2147098571
Cited by
295
References
4
FWCI
11.99
Type
journal article
Language
en
Open access
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CoChat. (2026). Citation check: 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. https://app.cochat.ai/papers/10.1073/pnas.96.16.8967
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Chen, J., Skehel, J. J., & Wiley, D. C. (1999). 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. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.16.8967

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