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1HTM

STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION

Summary for 1HTM
Entry DOI10.2210/pdb1htm/pdb
DescriptorHEMAGGLUTININ HA1 CHAIN, HEMAGGLUTININ HA2 CHAIN (3 entities in total)
Functional Keywordsinfluenza virus hemagglutinin, viral protein
Biological sourceuncultured beta proteobacterium UMTRA-608
More
Cellular locationVirion membrane; Single-pass type I membrane protein (Potential): P03437 P03437
Total number of polymer chains6
Total formula weight57132.57
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 citationBullough, 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: 8072525
DOI: 10.1038/371037a0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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