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4WSR

The crystal structure of hemagglutinin form A/chicken/New York/14677-13/1998

Summary for 4WSR
Entry DOI10.2210/pdb4wsr/pdb
Related4WSS 4WST 4WSU 4WSV 4WSW 4WSX
DescriptorHemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsinfluenza virus, hemagglutinin, h6, viral protein
Biological sourceInfluenza A virus (A/chicken/New York/14677-13/1998(H6N2))
Total number of polymer chains6
Total formula weight350925.26
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: 2024-10-09)
Primary citationYang, 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: 25673707
DOI: 10.1128/JVI.03456-14
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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