6TZB
Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin in complex with 6'-SLNLN
Summary for 6TZB
| Entry DOI | 10.2210/pdb6tzb/pdb |
| Related PRD ID | PRD_900046 |
| Descriptor | Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
| Functional Keywords | viral protein |
| Biological source | Influenza A virus (strain A/Hong Kong/1/1968 H3N2) More |
| Total number of polymer chains | 6 |
| Total formula weight | 174944.99 |
| Authors | Wu, N.C.,Wilson, I.A. (deposition date: 2019-08-12, release date: 2019-10-30, Last modification date: 2024-11-13) |
| Primary citation | Wu, N.C.,Otwinowski, J.,Thompson, A.J.,Nycholat, C.M.,Nourmohammad, A.,Wilson, I.A. Major antigenic site B of human influenza H3N2 viruses has an evolving local fitness landscape. Nat Commun, 11:1233-1233, 2020 Cited by PubMed Abstract: Antigenic drift of influenza virus hemagglutinin (HA) is enabled by facile evolvability. However, HA antigenic site B, which has become immunodominant in recent human H3N2 influenza viruses, is also evolutionarily constrained by its involvement in receptor binding. Here, we employ deep mutational scanning to probe the local fitness landscape of HA antigenic site B in six different human H3N2 strains spanning from 1968 to 2016. We observe that the fitness landscape of HA antigenic site B can be very different between strains. Sequence variants that exhibit high fitness in one strain can be deleterious in another, indicating that the evolutionary constraints of antigenic site B have changed over time. Structural analysis suggests that the local fitness landscape of antigenic site B can be reshaped by natural mutations via modulation of the receptor-binding mode. Overall, these findings elucidate how influenza virus continues to explore new antigenic space despite strong functional constraints. PubMed: 32144244DOI: 10.1038/s41467-020-15102-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.243 Å) |
Structure validation
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