4juh

From Proteopedia

Revision as of 19:13, 7 August 2013

Template:STRUCTURE 4juh

Crystal structure of 1918 pandemic influenza virus hemagglutinin mutant D225G complexed with avian receptor analogue LSTa

Template:ABSTRACT PUBMED 23514882

Function

[HEMA_I18A0] 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).

About this Structure

4juh is a 6 chain structure with sequence from Influenza a virus (a/south carolina/1/1918(h1n1)). Full crystallographic information is available from OCA.

Reference

• Zhang W, Shi Y, Qi J, Gao F, Li Q, Fan Z, Yan J, Gao GF. Molecular Basis of the Receptor Binding Specificity Switch of the Hemagglutinins from both the 1918 and 2009 Pandemic Influenza A Viruses by a D225G Substitution. J Virol. 2013 May;87(10):5949-58. doi: 10.1128/JVI.00545-13. Epub 2013 Mar 20. PMID:23514882 doi:10.1128/JVI.00545-13