4hg4
Crystal structure of Fab 2G1 in complex with a H2N2 influenza virus hemagglutininCrystal structure of Fab 2G1 in complex with a H2N2 influenza virus hemagglutinin
FunctionFunction
[Q67085_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
4hg4 is a 36 chain structure with sequence from Homo sapiens and Influenza a virus (a/japan/305+/1957(h2n2)). Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Xu R, Krause JC, McBride R, Paulson JC, Crowe JE Jr, Wilson IA. A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin. Nat Struct Mol Biol. 2013 Mar;20(3):363-70. doi: 10.1038/nsmb.2500. Epub 2013 Feb, 10. PMID:23396351 doi:10.1038/nsmb.2500