4mhh
Crystal structure of Fab H5M9 in complex with influenza virus hemagglutinin from A/Viet Nam/1203/2004 (H5N1)Crystal structure of Fab H5M9 in complex with influenza virus hemagglutinin from A/Viet Nam/1203/2004 (H5N1)
Template:ABSTRACT PUBMED 24049169
FunctionFunction
[Q6DQ33_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
4mhh is a 12 chain structure with sequence from Influenza a virus (a/viet nam/1203/2004(h5n1)) and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Zhu X, Guo YH, Jiang T, Wang YD, Chan KH, Li XF, Yu W, McBride R, Paulson JC, Yuen KY, Qin CF, Che XY, Wilson IA. A Unique and Conserved Neutralization Epitope in H5N1 Influenza Viruses Identified by a Murine Antibody against the A/goose/Guangdong/1/96 Hemagglutinin. J Virol. 2013 Sep 18. PMID:24049169 doi:10.1128/JVI.01577-13