4bh2
Crystal Structure of the Haemagglutinin from a Transmissible Mutant H5 Influenza VirusCrystal Structure of the Haemagglutinin from a Transmissible Mutant H5 Influenza Virus
Template:ABSTRACT PUBMED 23615615
FunctionFunction
[Q5EP31_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:SAAS008980_004_327643]
About this StructureAbout this Structure
4bh2 is a 2 chain structure with sequence from Influenza a virus (a/viet nam/1203/2004(h5n1)). Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Xiong X, Coombs PJ, Martin SR, Liu J, Xiao H, McCauley JW, Locher K, Walker PA, Collins PJ, Kawaoka Y, Skehel JJ, Gamblin SJ. Receptor binding by a ferret-transmissible H5 avian influenza virus. Nature. 2013 Apr 24. doi: 10.1038/nature12144. PMID:23615615 doi:10.1038/nature12144