title: Structure of influenza haemagglutinin at the pH of membrane fusion.
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 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
authors.forename: P A
authors.initials: PA
authors.lastname: Bullough
authors.forename: F M
authors.initials: FM
authors.lastname: Hughson
authors.forename: J J
authors.initials: JJ
authors.lastname: Skehel
authors.forename: D C
authors.initials: DC
authors.lastname: Wiley
mesh_terms: 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
chemical_list: D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D010446:Peptide Fragments