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Article| Volume 73, ISSUE 4, P823-832, May 21, 1993

A spring-loaded mechanism for the conformational change of influenza hemagglutinin

  • Chavela M. Carr
    Affiliations
    Howard Hughes Medical Institute Whitehead Institute for Biomedical Research Department of Biology Massachusetts Institute of Technology Cambridge, Massachusetts 02142 USA
    Search for articles by this author
  • Peter S. Kim
    Affiliations
    Howard Hughes Medical Institute Whitehead Institute for Biomedical Research Department of Biology Massachusetts Institute of Technology Cambridge, Massachusetts 02142 USA
    Search for articles by this author
DOI:https://doi.org/10.1016/0092-8674(93)90260-W
A spring-loaded mechanism for the conformational change of influenza hemagglutinin
Previous ArticleSolution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase

      Abstract

      Influenza hemagglutinin (HA) undergoes a conformational change that induces viral fusion with the cellular membrane. The structure of HA in the fusogenic state is unknown. We have identified a sequence in HA that has a high propensity for forming a coiled coil. Surprisingly, this sequence corresponds to a loop region in the X-ray structure of native HA: the loop is followed by a three-stranded, coiled-coil stem. We find that a 36 residue peptide (LOOP-36), comprising the loop region and the first part of the stem, forms a three-stranded coiled coil. This coiled coil is extended and stabilized in a longer peptide, corresponding to LOOP-36 plus the residues of a preceding, short α helix. These findings lead to a model for the fusogenic conformation of HA: the coiled-coil stem of the native state extends, relocating the hydrophobic fusion peptide, by 100 Å, toward the target membrane.
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      Article Info

      Publication History

      Received in revised form: April 9, 1993
      Received: February 5, 1993

      Identification

      DOI: https://doi.org/10.1016/0092-8674(93)90260-W

      Copyright

      © 1993 Published by Elsevier Inc.

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