2rft | pdb_00002rft
Crystal structure of influenza B virus hemagglutinin in complex with LSTa receptor analog
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| 2rft, resolution 2.80Å | |||||||||||||
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| Sites: | AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9, BC1, BC2, BC3, BC4 and BC5 | ||||||||||||
| Ligands: | BGC, GAL, NAG, NDG, SIA | ||||||||||||
| Gene: | Hemagglutinin (Influenza B virus) | ||||||||||||
| Related: | 2RFU
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
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