4m4y
Crystal structure of a 2009 H1N1 influenza virus hemagglutinin with a stabilization mutation HA2 E47GCrystal structure of a 2009 H1N1 influenza virus hemagglutinin with a stabilization mutation HA2 E47G
Template:ABSTRACT PUBMED 24027321
FunctionFunction
[C3W5S1_I09A0] 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).[SAAS:SAAS013829_004_327643][RuleBase:RU003324]
About this StructureAbout this Structure
4m4y is a 6 chain structure with sequence from Influenza a virus (a/california/04/2009(h1n1)). Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Hong M, Lee PS, Hoffman RM, Zhu X, Krause JC, Laursen NS, Yoon SI, Song L, Tussey L, Crowe JE Jr, Ward AB, Wilson IA. Antibody Recognition of the Pandemic H1N1 Influenza Hemagglutinin Receptor Binding Site. J Virol. 2013 Sep 11. PMID:24027321 doi:10.1128/JVI.01388-13