Structural highlights
Publication Abstract from PubMed
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.
Structure of influenza haemagglutinin at the pH of membrane fusion.,Bullough PA, Hughson FM, Skehel JJ, Wiley DC Nature. 1994 Sep 1;371(6492):37-43. PMID:8072525[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bullough PA, Hughson FM, Skehel JJ, Wiley DC. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature. 1994 Sep 1;371(6492):37-43. PMID:8072525 doi:http://dx.doi.org/10.1038/371037a0
