STRUCTURE OF INFLUENZA HEMAGGLUTININ AT THE PH OF MEMBRANE-FUSION

Article

关键词: VIRUS HEMAGGLUTININ;    CONFORMATIONAL CHANGE;    PROTEIN MODELS;    ACTIVATION;    ACID;    GLYCOPROTEIN;    ANTIBODIES;    HEMOLYSIS;    MECHANISM;    RESOLUTION;   

DOI  :  10.1038/371037a0

来源: SCIE

【 摘 要 】

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 Angstrom 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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