4i78
From Proteopedia
Contents |
Crystal structure of a subtype H17 hemagglutinin homologue from A/little yellow-shouldered bat/Guatemala/060/2010 (H17N10)
Template:ABSTRACT PUBMED 23297216
Function
[H6QM93_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]
About this Structure
4i78 is a 4 chain structure with sequence from Influenza a virus (a/little yellow-shouldered bat/guatemala/060/2010(h17n10)). Full crystallographic information is available from OCA.
Reference
- Zhu X, Yu W, McBride R, Li Y, Chen LM, Donis RO, Tong S, Paulson JC, Wilson IA. Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities. Proc Natl Acad Sci U S A. 2013 Jan 7. PMID:23297216 doi:10.1073/pnas.1218509110
