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{{STRUCTURE_4nrk| PDB=4nrk | SCENE= }} | |||
===Structure of hemagglutinin with F95Y mutation of influenza virus B/Lee/40 complex with LSTc=== | |||
{{ABSTRACT_PUBMED_24503069}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/HEMA_INBLE HEMA_INBLE]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. | |||
==About this Structure== | |||
[[4nrk]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRK OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024503069</ref><references group="xtra"/><references/> | |||
[[Category: Kondrashkina, E.]] | |||
[[Category: Mbawuike, I N.]] | |||
[[Category: Ni, F.]] | |||
[[Category: Wang, Q.]] | |||
[[Category: Ha]] | |||
[[Category: Viral protein]] | |||
Revision as of 16:39, 12 March 2014
Structure of hemagglutinin with F95Y mutation of influenza virus B/Lee/40 complex with LSTcStructure of hemagglutinin with F95Y mutation of influenza virus B/Lee/40 complex with LSTc
Template:ABSTRACT PUBMED 24503069
FunctionFunction
[HEMA_INBLE] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
About this StructureAbout this Structure
4nrk is a 6 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Ni F, Nnadi Mbawuike I, Kondrashkina E, Wang Q. The roles of hemagglutinin Phe-95 in receptor binding and pathogenicity of influenza B virus. Virology. 2014 Feb;450-451:71-83. doi: 10.1016/j.virol.2013.11.038. Epub 2013 Dec, 22. PMID:24503069 doi:http://dx.doi.org/10.1016/j.virol.2013.11.038