2RFU: Crystal Structure Of Influenza B Virus Hemagglutinin In Complex With Lstc Receptor Analog

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.
PDB ID: 2RFUDownload
MMDB ID: 62246
PDB Deposition Date: 2007/10/1
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Similar Structures:
Biological Unit for 2RFU: hexameric; determined by author and by software (PISA)
Molecular Components in 2RFU
Label Count Molecule
Proteins (6 molecules)
Influenza B Hemagglutinin (Ha)
Molecule annotation
Influenza B Hemagglutinin (Ha)
Molecule annotation
Chemicals (27 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB