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4LKJ

The structure of hemagglutinin L226Q mutant (H3 numbering) from a avian-origin H7N9 influenza virus (A/Anhui/1/2013) in complex with avian receptor analog 3'SLNLN

Summary for 4LKJ
Entry DOI10.2210/pdb4lkj/pdb
Related4LKG 4LKH 4LKI 4LKK
Related PRD IDPRD_900067
Descriptorhemagglutinin, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordshomotrimer, virus attachment, membrane fusion, viral protein
Biological sourceInfluenza A virus
More
Total number of polymer chains2
Total formula weight54982.04
Authors
Shi, Y.,Zhang, W.,Wang, F.,Qi, J.,Song, H.,Wu, Y.,Gao, F.,Zhang, Y.,Fan, Z.,Gong, W.,Wang, D.,Shu, Y.,Wang, Y.,Yan, J.,Gao, G.F. (deposition date: 2013-07-07, release date: 2013-11-06, Last modification date: 2024-11-06)
Primary citationShi, 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: 24009358
DOI: 10.1126/science.1242917
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.798 Å)
Structure validation

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数据于2024-11-06公开中

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