Structure of influenza haemagglutinin at the pH of membrane fusion.
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 A 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.
Bullough
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PA
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
Hughson
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Skehel
J J
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Wiley
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D000595:Amino Acid Sequence; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000737:chemistry* / Q000648:ultrastructure; D006863:Hydrogen-Ion Concentration; D008561:Membrane Fusion; D008969:Molecular Sequence Data; D009154:Mutation; D009975:Orthomyxoviridae / Q000737:chemistry / Q000648:ultrastructure; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D010446:Peptide Fragments