Abstract
The three‐dimensional structures of the complete haemagglutinin (HA) of influenza virus A/Japan/305/57 (H2N2) in its native (neutral pH) and membrane fusion‐competent (low pH) form by electron cryo‐microscopy at a resolution of 10 Å and 14 Å, respectively, have been determined. In the fusion‐competent form the subunits remain closely associated preserving typical overall features of the trimeric ectodomain at neutral pH. Rearrangements of the tertiary structure in the distal and the stem parts are associated with the formation of a central cavity through the entire ectodomain. We suggest that the cavity is essential for relocation of the so‐called fusion sequence of HA towards the target membrane.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 3:16 p.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 3:44 p.m.) |
Indexed | 1 month, 1 week ago (July 19, 2025, 11:26 p.m.) |
Issued | 25 years, 8 months ago (Dec. 17, 1999) |
Published | 25 years, 8 months ago (Dec. 17, 1999) |
Published Online | 25 years, 7 months ago (Jan. 18, 2000) |
Published Print | 25 years, 8 months ago (Dec. 17, 1999) |
@article{B_ttcher_1999, title={Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo‐microscopy}, volume={463}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(99)01475-1}, DOI={10.1016/s0014-5793(99)01475-1}, number={3}, journal={FEBS Letters}, publisher={Wiley}, author={Böttcher, Christoph and Ludwig, Kai and Herrmann, Andreas and van Heel, Marin and Stark, Holger}, year={1999}, month=dec, pages={255–259} }