6PCX
Crystal Structure of a H5N1 influenza virus hemagglutinin at pH 6.0
Summary for 6PCX
| Entry DOI | 10.2210/pdb6pcx/pdb |
| Descriptor | Hemagglutinin, SULFATE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | influenza, h5, viral protein |
| Biological source | Influenza A virus (A/mallard/Vietnam/3/2003(H5N1)) |
| Total number of polymer chains | 1 |
| Total formula weight | 62150.09 |
| Authors | Antanasijevic, A.,Durst, M.A.,Lavie, A.,Caffrey, M. (deposition date: 2019-06-18, release date: 2019-11-13, Last modification date: 2023-10-11) |
| Primary citation | Antanasijevic, A.,Durst, M.A.,Lavie, A.,Caffrey, M. Identification of a pH sensor in Influenza hemagglutinin using X-ray crystallography. J.Struct.Biol., 209:107412-107412, 2020 Cited by PubMed Abstract: Hemagglutnin (HA) mediates entry of influenza virus through a series of conformational changes triggered by the low pH of the endosome. The residue or combination of residues acting as pH sensors has not yet been fully elucidated. In this work, we assay pH effects on the structure of H5 HA by soaking HA crystallized at pH 6.5 in a series of buffers with lower pH, mimicking the conditions of the endosome. We find that HA1-H38, which is conserved in Group 1 HA, undergoes a striking change in side chain conformation, which we attribute to its protonation and cation-cation repulsion with conserved HA1-H18. This work suggests that x-ray crystallography can be applied for studying small-scale pH-induced conformational changes providing valuable information on the location of pH sensors in HA. Importantly, the observed change in HA1-H38 conformation is further evidence that the pH-induced conformational changes of HA are the result of a series of protonation events to conserved and non-conserved pH sensors. PubMed: 31689502DOI: 10.1016/j.jsb.2019.107412 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.11 Å) |
Structure validation
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