Structure of influenza haemagglutinin at the pH of membrane fusion

Per A. Bullough, Frederick M. Hughson, John J. Skehel, Don C. Wiley

Research output: Contribution to journalArticlepeer-review

1398 Scopus citations

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 Å 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.

Original languageEnglish (US)
Pages (from-to)37-43
Number of pages7
JournalNature
Volume371
Issue number6492
DOIs
StatePublished - 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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