2rft

From Proteopedia

Revision as of 06:14, 13 February 2008

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

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