2RFT

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

Summary for 2RFT

• Entry DOI: 10.2210/pdb2rft/pdb
• Related: 2RFU
• Descriptor: Influenza B hemagglutinin (HA), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: influenza, viral protein, receptor specificity, envelope protein, fusion protein, hemagglutinin, membrane, transmembrane, virion, glycoprotein, lipoprotein, palmitate
• Biological source: Influenza B virus (STRAIN B/HONG KONG/8/73); More
• Total number of polymer chains: 2
• Total formula weight: 59469.93

Authors

Wang, Q.,Tian, X.,Chen, X.,Ma, J. (deposition date: 2007-10-01, release date: 2008-02-05, Last modification date: 2024-10-30)

Primary citation

Wang, Q.,Tian, X.,Chen, X.,Ma, J.
Structural basis for receptor specificity of influenza B virus hemagglutinin.
Proc.Natl.Acad.Sci.Usa, 104:16874-16879, 2007

PubMed Abstract: 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.

PubMed: 17942670
DOI: 10.1073/pnas.0708363104

Experimental method

X-RAY DIFFRACTION (2.8 Å)