2rft: Difference between revisions

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[[Image:2rft.jpg|left|200px]]
{{Seed}}
[[Image:2rft.png|left|200px]]


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{{STRUCTURE_2rft|  PDB=2rft  |  SCENE=  }}  
{{STRUCTURE_2rft|  PDB=2rft  |  SCENE=  }}  


'''Crystal structure of influenza B virus hemagglutinin in complex with LSTa receptor analog'''
===Crystal structure of influenza B virus hemagglutinin in complex with LSTa receptor analog===




==Overview==
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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.
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{{ABSTRACT_PUBMED_17942670}}


==About this Structure==
==About this Structure==
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[[Category: Viral protein]]
[[Category: Viral protein]]
[[Category: Virion]]
[[Category: Virion]]
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