Structure of influenza haemagglutinin at the pH of membrane fusion View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-09

AUTHORS

P A Bullough, F M Hughson, J J Skehel, D C Wiley

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. More... »

PAGES

37-43

Journal

TITLE

Nature

ISSUE

6492

VOLUME

371

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/371037a0

    DOI

    http://dx.doi.org/10.1038/371037a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1046282624

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/8072525


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