4CQZ: Crystal Structure Of H5 (vn1194) Gln196arg Mutant Haemagglutinin

Citation:
Abstract
Mutant H5N1 influenza viruses have been isolated from humans that have increased human receptor avidity. We have compared the receptor binding properties of these mutants with those of wild-type viruses, and determined the structures of their haemagglutinins in complex with receptor analogues. Mutants from Vietnam bind tighter to human receptor by acquiring basic residues near the receptor binding site. They bind more weakly to avian receptor because they lack specific interactions between Asn-186 and Gln-226. In contrast, a double mutant, Delta133/Ile155Thr, isolated in Egypt has greater avidity for human receptor while retaining wild-type avidity for avian receptor. Despite these increases in human receptor binding, none of the mutants prefers human receptor, unlike aerosol transmissible H5N1 viruses. Nevertheless, mutants with high avidity for both human and avian receptors may be intermediates in the evolution of H5N1 viruses that could infect both humans and poultry.
PDB ID: 4CQZDownload
MMDB ID: 120241
PDB Deposition Date: 2014/2/21
Updated in MMDB: 2014/06
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 4CQZ: hexameric; determined by author and by software (PISA)
Molecular Components in 4CQZ
Label Count Molecule
Proteins (6 molecules)
3
Haemagglutinin HA1
Molecule annotation
3
Haemagglutinin HA2
Molecule annotation
Chemicals (21 molecules)
1
3
2
3
3
12
4
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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