5XHV
Crystal Structure Of Fab S40 In Complex With Influenza Hemagglutinin, HA1 subunit.
Summary for 5XHV
Entry DOI | 10.2210/pdb5xhv/pdb |
Descriptor | Hemagglutinin, S40 heavy chain, S40 light chain (3 entities in total) |
Functional Keywords | viral protein-immune system, viral protein-immune system complex, viral protein/immune system |
Biological source | Influenza A virus (A/California/07/2009(H1N1)) More |
Cellular location | Host apical cell membrane ; Single-pass type I membrane protein . Virion membrane ; Single-pass type I membrane protein : C3W5X2 |
Total number of polymer chains | 6 |
Total formula weight | 168100.17 |
Authors | Lee, C.C.,Wang, A.H.J.,Yu, C.M.,Yang, A.S. (deposition date: 2017-04-24, release date: 2017-11-15, Last modification date: 2024-10-23) |
Primary citation | Chen, I.C.,Chiu, Y.K.,Yu, C.M.,Lee, C.C.,Tung, C.P.,Tsou, Y.L.,Huang, Y.J.,Lin, C.L.,Chen, H.S.,Wang, A.H.,Yang, A.S. High throughput discovery of influenza virus neutralizing antibodies from phage-displayed synthetic antibody libraries. Sci Rep, 7:14455-14455, 2017 Cited by PubMed Abstract: Pandemic and epidemic outbreaks of influenza A virus (IAV) infection pose severe challenges to human society. Passive immunotherapy with recombinant neutralizing antibodies can potentially mitigate the threats of IAV infection. With a high throughput neutralizing antibody discovery platform, we produced artificial anti-hemagglutinin (HA) IAV-neutralizing IgGs from phage-displayed synthetic scFv libraries without necessitating prior memory of antibody-antigen interactions or relying on affinity maturation essential for in vivo immune systems to generate highly specific neutralizing antibodies. At least two thirds of the epitope groups of the artificial anti-HA antibodies resemble those of natural protective anti-HA antibodies, providing alternatives to neutralizing antibodies from natural antibody repertoires. With continuing advancement in designing and constructing synthetic scFv libraries, this technological platform is useful in mitigating not only the threats of IAV pandemics but also those from other newly emerging viral infections. PubMed: 29089574DOI: 10.1038/s41598-017-14823-w PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.35 Å) |
Structure validation
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