1HTM
STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION
Summary for 1HTM
Entry DOI | 10.2210/pdb1htm/pdb |
Descriptor | HEMAGGLUTININ HA1 CHAIN, HEMAGGLUTININ HA2 CHAIN (3 entities in total) |
Functional Keywords | influenza virus hemagglutinin, viral protein |
Biological source | uncultured beta proteobacterium UMTRA-608 More |
Cellular location | Virion membrane; Single-pass type I membrane protein (Potential): P03437 P03437 |
Total number of polymer chains | 6 |
Total formula weight | 57132.57 |
Authors | Bullough, P.A.,Hughson, F.M.,Skehel, J.J.,Wiley, D.C. (deposition date: 1994-11-02, release date: 1995-02-14, Last modification date: 2024-10-30) |
Primary citation | Bullough, P.A.,Hughson, F.M.,Skehel, J.J.,Wiley, D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature, 371:37-43, 1994 Cited by PubMed 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. PubMed: 8072525DOI: 10.1038/371037a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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