4K62: Structure Of An Avian Influenza H5 Hemagglutinin From The Influenza Virus A/indonesia/5/2005

Recent studies have identified several mutations in the hemagglutinin (HA) protein that allow the highly pathogenic avian H5N1 influenza A virus to transmit between mammals by airborne route. Here, we determined the complex structures of wild-type and mutant HAs derived from an Indonesia H5N1 virus bound to either avian or human receptor sialic acid analogs. A cis/trans conformational change in the glycosidic linkage of the receptor analog was observed, which explains how the H5N1 virus alters its receptor binding preference. Furthermore, the mutant HA possessed low affinities for both avian and human receptors. Our findings provide a structural and biophysical basis for the H5N1 adaptation to acquire human, but maintain avian, receptor binding properties.
PDB ID: 4K62Download
MMDB ID: 110342
PDB Deposition Date: 2013/4/15
Updated in MMDB: 2013/05
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 4K62: hexameric; determined by author and by software (PISA)
Molecular Components in 4K62
Label Count Molecule
Proteins (6 molecules)
Molecule annotation
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB