3KU6
Crystal structure of a H2N2 influenza virus hemagglutinin, 226L/228G
Summary for 3KU6
| Entry DOI | 10.2210/pdb3ku6/pdb |
| Related | 3KU3 3KU5 |
| Descriptor | Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | viral envelope protein, hemagglutinin, viral fusion protein, envelope protein, viral protein |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 2 |
| Total formula weight | 57442.35 |
| Authors | Xu, R.,Wilson, I.A. (deposition date: 2009-11-26, release date: 2010-01-19, Last modification date: 2021-10-13) |
| Primary citation | Xu, R.,McBride, R.,Paulson, J.C.,Basler, C.F.,Wilson, I.A. Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic. J.Virol., 84:1715-1721, 2010 Cited by PubMed Abstract: The hemagglutinin (HA) envelope protein of influenza viruses mediates essential viral functions, including receptor binding and membrane fusion, and is the major viral antigen for antibody neutralization. The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused 1 million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60 to 1.75 A resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with the results of glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding sites were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in the design of a broader and more universal influenza A virus vaccine. PubMed: 20007271DOI: 10.1128/JVI.02162-09 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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