4LCX
The structure of hemagglutinin from avian-origin H7N9 influenza virus (A/Shanghai/1/2013)
Summary for 4LCX
Entry DOI | 10.2210/pdb4lcx/pdb |
Related | 4KOL 4KOM 4KON |
Descriptor | Hemagglutinin HA1, Hemagglutinin HA2, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | homotrimer, virus attachment and membrane fusion, viral protein |
Biological source | Influenza A virus More |
Total number of polymer chains | 6 |
Total formula weight | 163024.45 |
Authors | |
Primary citation | Shi, Y.,Zhang, W.,Wang, F.,Qi, J.,Wu, Y.,Song, H.,Gao, F.,Bi, Y.,Zhang, Y.,Fan, Z.,Qin, C.,Sun, H.,Liu, J.,Haywood, J.,Liu, W.,Gong, W.,Wang, D.,Shu, Y.,Wang, Y.,Yan, J.,Gao, G.F. Structures and receptor binding of hemagglutinins from human-infecting H7N9 influenza viruses. Science, 342:243-247, 2013 Cited by PubMed Abstract: An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln(226)) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature residue Leu(226)). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (Leu(226) → Gln) was found to exhibit dual receptor-binding property, indicating that other amino acid substitutions contribute to the receptor-binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how AH-H7N9 can bind human receptors while still retaining the avian receptor-binding property. PubMed: 24009358DOI: 10.1126/science.1242917 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.094 Å) |
Structure validation
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