Abstract
Low pH induces a conformational change in the influenza virus haemagglutinin, which then mediates fusion of the viral and host cell membranes. The three-dimensional structure of a fragment of the haemagglutinin in this conformation reveals a major refolding of the secondary and tertiary structure of the molecule. The apolar fusion peptide moves at least 100 Å to one tip of the molecule. At the other end a helical segment unfolds, a subdomain relocates reversing the chain direction, and part of the structure becomes disordered.
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Bullough, P., Hughson, F., Skehel, J. et al. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37–43 (1994). https://doi.org/10.1038/371037a0
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DOI: https://doi.org/10.1038/371037a0
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