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{{STRUCTURE_2rfu| PDB=2rfu | SCENE= }} | |||
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'''Crystal structure of influenza B virus hemagglutinin in complex with LSTc receptor analog''' | '''Crystal structure of influenza B virus hemagglutinin in complex with LSTc receptor analog''' | ||
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[[Category: Tian, X.]] | [[Category: Tian, X.]] | ||
[[Category: Wang, Q.]] | [[Category: Wang, Q.]] | ||
[[Category: | [[Category: Envelope protein]] | ||
[[Category: | [[Category: Fusion protein]] | ||
[[Category: | [[Category: Glycoprotein]] | ||
[[Category: | [[Category: Hemagglutinin]] | ||
[[Category: | [[Category: Human receptor analog]] | ||
[[Category: | [[Category: Influenza]] | ||
[[Category: | [[Category: Lipoprotein]] | ||
[[Category: | [[Category: Membrane]] | ||
[[Category: | [[Category: Palmitate]] | ||
[[Category: | [[Category: Receptor specificity]] | ||
[[Category: | [[Category: Transmembrane]] | ||
[[Category: | [[Category: Viral protein]] | ||
[[Category: | [[Category: Virion]] | ||
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Revision as of 13:50, 4 May 2008
Crystal structure of influenza B virus hemagglutinin in complex with LSTc receptor analog
Overview
Receptor-binding specificity of HA, the major surface glycoprotein of influenza virus, primarily determines the host ranges that the virus can infect. Influenza type B virus almost exclusively infects humans and contributes to the annual "flu" sickness. Here we report the structures of influenza B virus HA in complex with human and avian receptor analogs, respectively. These structures provide a structural basis for the different receptor-binding properties of influenza A and B virus HA molecules and for the ability of influenza B virus HA to distinguish human and avian receptors. The structure of influenza B virus HA with avian receptor analog also reveals how mutations in the region of residues 194 to 196, which are frequently observed in egg-adapted and naturally occurring variants, directly affect the receptor binding of the resultant virus strains. Furthermore, these structures of influenza B virus HA are compared with known structures of influenza A virus HAs, which suggests the role of the residue at 222 as a key and likely a universal determinant for the different binding modes of human receptor analogs by different HA molecules.
About this Structure
2RFU is a Protein complex structure of sequences from Influenza b virus. Full crystallographic information is available from OCA.
Reference
Structural basis for receptor specificity of influenza B virus hemagglutinin., Wang Q, Tian X, Chen X, Ma J, Proc Natl Acad Sci U S A. 2007 Oct 23;104(43):16874-9. Epub 2007 Oct 17. PMID:17942670 Page seeded by OCA on Sun May 4 16:50:50 2008
