3BT6
Crystal Structure of Influenza B Virus Hemagglutinin
Summary for 3BT6
| Entry DOI | 10.2210/pdb3bt6/pdb |
| Related | 2RFT 2RFU |
| Descriptor | Influenza B hemagglutinin (HA), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | antigenic variation, membrane fusion, envelope protein, fusion protein, hemagglutinin, transmembrane, virion, glycoprotein, lipoprotein, palmitate, viral protein |
| Biological source | Influenza B virus More |
| Total number of polymer chains | 2 |
| Total formula weight | 57610.04 |
| Authors | |
| Primary citation | Wang, Q.,Cheng, F.,Lu, M.,Tian, X.,Ma, J. Crystal structure of unliganded influenza B virus hemagglutinin. J.Virol., 82:3011-3020, 2008 Cited by PubMed Abstract: Here we report the crystal structure of hemagglutinin (HA) from influenza B/Hong Kong/8/73 (B/HK) virus determined to 2.8 A. At a sequence identity of approximately 25% to influenza A virus HAs, B/HK HA shares a similar overall structure and domain organization. More than two dozen amino acid substitutions on influenza B virus HAs have been identified to cause antigenicity alteration in site-specific mutants, monoclonal antibody escape mutants, or field isolates. Mapping these substitutions on the structure of B/HK HA reveals four major epitopes, the 120 loop, the 150 loop, the 160 loop, and the 190 helix, that are located close in space to form a large, continuous antigenic site. Moreover, a systematic comparison of known HA structures across the entire influenza virus family reveals evolutionarily conserved ionizable residues at all regions along the chain and subunit interfaces. These ionizable residues are likely the structural basis for the pH dependence and sensitivity to ionic strength of influenza HA and hemagglutinin-esterase fusion proteins. PubMed: 18184701DOI: 10.1128/JVI.02477-07 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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