3HTQ
the hemagglutinin structure of an avian H1N1 influenza A virus in complex with LSTc
Summary for 3HTQ
| Entry DOI | 10.2210/pdb3htq/pdb |
| Related | 3HTO 3HTP 3HTT |
| Descriptor | Hemagglutinin, Hemagglutinin HA2 chain, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | receptor, viral protein |
| Biological source | Influenza A virus (A/WDK/JX/12416/2005(H1N1)) (A/WDK/JX/12416/2005(H1N1)) More |
| Total number of polymer chains | 2 |
| Total formula weight | 55572.62 |
| Authors | |
| Primary citation | Lin, T.,Wang, G.,Li, A.,Zhang, Q.,Wu, C.,Zhang, R.,Cai, Q.,Song, W.,Yuen, K.-Y. The hemagglutinin structure of an avian H1N1 influenza A virus Virology, 392:73-81, 2009 Cited by PubMed Abstract: The interaction between hemagglutinin (HA) and receptors is a kernel in the study of evolution and host adaptation of H1N1 influenza A viruses. The notion that the avian HA is associated with preferential specificity for receptors with Siaalpha2,3Gal glycosidic linkage over those with Siaalpha2,6Gal linkage is not all consistent with the available data on H1N1 viruses. By x-ray crystallography, the HA structure of an avian H1N1 influenza A virus, as well as its complexes with the receptor analogs, was determined. The structures revealed no preferential binding of avian receptor analogs over that of the human analog, suggesting that the HA/receptor binding might not be as stringent as is commonly believed in determining the host receptor preference for some subtypes of influenza viruses, such as the H1N1 viruses. The structure also showed difference in glycosylation despite the preservation of related sequences, which may partly contribute to the difference between structures of human and avian origin. PubMed: 19628241DOI: 10.1016/j.virol.2009.06.028 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.955 Å) |
Structure validation
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