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 language | English (US) |
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Pages (from-to) | 37-43 |
Number of pages | 7 |
Journal | Nature |
Volume | 371 |
Issue number | 6492 |
DOIs | |
State | Published - 1994 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- General