4EDA
Structures of monomeric hemagglutinin and its complex with an Fab fragment of a neutralizing antibody that binds to H1 subtype influenza viruses: molecular basis of infectivity of 2009 pandemic H1N1 influenza A viruses
Summary for 4EDA
| Entry DOI | 10.2210/pdb4eda/pdb |
| Related | 4EDB |
| Descriptor | Hemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | influenza virus, haemagglutinin, conformation, antibody, viral protein |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 4 |
| Total formula weight | 118104.02 |
| Authors | Kim, K.H.,Cho, K.J.,Lee, J.H.,Park, Y.H.,Khan, T.G.,Lee, J.Y.,Kang, S.H.,Alam, I. (deposition date: 2012-03-27, release date: 2013-05-22, Last modification date: 2020-07-29) |
| Primary citation | Cho, K.J.,Lee, J.H.,Hong, K.W.,Kim, S.H.,Park, Y.,Lee, J.Y.,Kang, S.,Kim, S.,Yang, J.H.,Kim, E.K.,Seok, J.H.,Unzai, S.,Park, S.Y.,Saelens, X.,Kim, C.J.,Lee, J.Y.,Kang, C.,Oh, H.B.,Chung, M.S.,Kim, K.H. Insight into structural diversity of influenza virus haemagglutinin J.Gen.Virol., 94:1712-1722, 2013 Cited by PubMed Abstract: Influenza virus infects host cells through membrane fusion, a process mediated by the low pH-induced conformational change of the viral surface glycoprotein haemagglutinin (HA). We determined the structures and biochemical properties of the HA proteins from A/Korea/01/2009 (KR01), a 2009 pandemic strain, and A/Thailand/CU44/2006 (CU44), a seasonal strain. The crystal structure of KR01 HA revealed a V-shaped head-to-head arrangement, which is not seen in other HA proteins including CU44 HA. We isolated a broadly neutralizing H1-specific monoclonal antibody GC0757. The KR01 HA-Fab0757 complex structure also exhibited a head-to-head arrangement of HA. Both native and Fab complex structures reveal a different spatial orientation of HA1 relative to HA2, indicating that HA is flexible and dynamic at neutral pH. Further, the KR01 HA exhibited significantly lower protein stability and increased susceptibility to proteolytic cleavage compared with other HAs. Our structures provide important insights into the conformational flexibility of HA. PubMed: 23636824DOI: 10.1099/vir.0.051136-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.701 Å) |
Structure validation
Download full validation report
