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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
Open accessAbstract
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
- green
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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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