3KU3
Crystal structure of a H2N2 influenza virus hemagglutinin, avian like
3KU3 の概要
| エントリーDOI | 10.2210/pdb3ku3/pdb |
| 関連するPDBエントリー | 3ku5 3ku6 |
| 分子名称 | 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) |
| 機能のキーワード | viral envelope protein, hemagglutinin, viral fusion protein, envelope protein, viral protein |
| 由来する生物種 | Influenza A virus 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 57881.72 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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