4WSX
The crystal structure of hemagglutinin from A/Jiangxi-Donghu/346/2013 influenza virus
Summary for 4WSX
| Entry DOI | 10.2210/pdb4wsx/pdb |
| Related | 4WSR 4WSS 4WST 4WSU 4WSV 4WSW |
| Descriptor | Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | hemagglutinin, influenza virus, h10, viral protein |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 24 |
| Total formula weight | 674035.49 |
| Authors | Yang, H.,Carney, P.J.,Chang, J.C.,Villanueva, J.M.,Stevens, J. (deposition date: 2014-10-28, release date: 2015-02-25, Last modification date: 2024-11-06) |
| Primary citation | Yang, H.,Carney, P.J.,Chang, J.C.,Villanueva, J.M.,Stevens, J. Structure and receptor binding preferences of recombinant hemagglutinins from avian and human h6 and h10 influenza a virus subtypes. J.Virol., 89:4612-4623, 2015 Cited by PubMed Abstract: During 2013, three new avian influenza A virus subtypes, A(H7N9), A(H6N1), and A(H10N8), resulted in human infections. While the A(H7N9) virus resulted in a significant epidemic in China across 19 provinces and municipalities, both A(H6N1) and A(H10N8) viruses resulted in only a few human infections. This study focuses on the major surface glycoprotein hemagglutinins from both of these novel human viruses. The detailed structural and glycan microarray analyses presented here highlight the idea that both A(H6N1) and A(H10N8) virus hemagglutinins retain a strong avian receptor binding preference and thus currently pose a low risk for sustained human infections. PubMed: 25673707DOI: 10.1128/JVI.03456-14 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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