6A4K
Human antibody 32D6 Fab in complex with H1N1 influenza A virus HA1
Summary for 6A4K
| Entry DOI | 10.2210/pdb6a4k/pdb |
| Descriptor | Hemagglutinin, immunoglobulin Fab heavy chain, immunoglobulin Fab light chain, ... (7 entities in total) |
| Functional Keywords | antibody fab, influenza hemagglutinin, complex structure, specific binding, viral protein-immune system complex, viral protein/immune system |
| Biological source | Influenza A virus (A/California/7/2009(H1N1)) (A/California/07/2009(H1N1)) More |
| Total number of polymer chains | 12 |
| Total formula weight | 301093.20 |
| Authors | Lee, C.C.,Ko, T.P.,Lin, L.L.,Wang, A.H.J. (deposition date: 2018-06-20, release date: 2019-03-27, Last modification date: 2024-10-23) |
| Primary citation | Lee, C.C.,Yang, C.Y.,Lin, L.L.,Ko, T.P.,Chang, A.H.,Chang, S.S.,Wang, A.H. An Effective Neutralizing Antibody Against Influenza Virus H1N1 from Human B Cells. Sci Rep, 9:4546-4546, 2019 Cited by PubMed Abstract: Influenza is a contagious acute respiratory disease caused by the influenza virus infection. Hemagglutinin (HA) is an important target in the therapeutic treatment and diagnostic detection of the influenza virus. Influenza A virus encompasses several different HA subtypes with different strains, which are constantly changing. In this study, we identified a fully human H1N1 neutralizing antibody (32D6) via an Epstein-Barr virus-immortalized B cell-based technology. 32D6 specifically neutralizes the clinically isolated H1N1 strains after the 2009 pandemic but not the earlier strains. The epitope was identified through X-ray crystallographic analysis of the 32D6-Fab/HA1 complex structure, which revealed a unique loop conformation located on the top surface of HA. The major region is composed of two peptide segments (residues 172-177 and 206-213), which form an abreast loop conformation. The residue T262 between the two loops forms a conformational epitope for recognition by 32D6. Three water molecules were observed at the interface of HA and the heavy chain, and they may constitute a stabilizing element for the 32D6-HA association. In addition, each 32D6-Fab is likely capable of blocking one HA trimer. This study provides important information on the strain specificity of 32D6 for the therapeutic treatment and detection of viral infection. PubMed: 30872685DOI: 10.1038/s41598-019-40937-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
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