3htt
The hemagglutinin structure of an avian H1N1 influenza A virus in complex with 2,3-sialyllactoseThe hemagglutinin structure of an avian H1N1 influenza A virus in complex with 2,3-sialyllactose
Template:ABSTRACT PUBMED 19628241
FunctionFunction
[C7C6F1_9INFA] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324][SAAS:SAAS013829_004_327643]
About this StructureAbout this Structure
3htt is a 2 chain structure with sequence from Influenza a virus (a/wdk/jx/12416/2005(h1n1)). Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Lin T, Wang G, Li A, Zhang Q, Wu C, Zhang R, Cai Q, Song W, Yuen KY. The hemagglutinin structure of an avian H1N1 influenza A virus. Virology. 2009 Sep 15;392(1):73-81. Epub 2009 Jul 22. PMID:19628241 doi:10.1016/j.virol.2009.06.028