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2rft
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Receptor-binding specificity of HA, the major surface glycoprotein of | + | 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== | ==About this Structure== | ||
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[[Category: virion]] | [[Category: virion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:47:03 2008'' |
Revision as of 16:47, 21 February 2008
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Crystal structure of influenza B virus hemagglutinin in complex with LSTa 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
2RFT is a Protein complex structure of sequences from Influenza b virus with as ligand. Known structural/functional Sites: , , , , , , , , , , , , and . 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 Thu Feb 21 18:47:03 2008
Categories: Influenza b virus | Protein complex | Chen, X. | Ma, J. | Tian, X. | Wang, Q. | NAG | Envelope protein | Fusion protein | Glycoprotein | Hemagglutinin | Influenza | Lipoprotein | Membrane | Palmitate | Receptor specificity | Transmembrane | Viral protein | Virion
