3m6s
From Proteopedia
Contents |
Crystal structure of H1N1pdm Hemagglutinin
Template:ABSTRACT PUBMED 20352039
Function
[C5MV42_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 Structure
3m6s is a 12 chain structure with sequence from Influenza a virus (a/darwin/2001/2009(h1n1)). Full crystallographic information is available from OCA.
See Also
Reference
- Yang H, Carney P, Stevens J. Structure and Receptor binding properties of a pandemic H1N1 virus hemagglutinin. PLoS Curr Influenza. 2010 Mar 22:RRN1152. PMID:20352039
