4N5Z

Crystal structure of aerosol transmissible influenza H5 hemagglutinin mutant (N158D, N224K, Q226L and T318I) from the influenza virus A/Viet Nam/1203/2004 (H5N1)

Summary for 4N5Z

• Entry DOI: 10.2210/pdb4n5z/pdb
• Related: 2FK0 4N5Y
• Descriptor: Hemagglutinin HA1 chain, Hemagglutinin, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: h5n1, influenza virus, hemagglutinin, viral protein, ferret transmissible
• Biological source: Influenza A virus; More
• Total number of polymer chains: 30
• Total formula weight: 895889.45

Authors

Zhu, X.,Wilson, I.A. (deposition date: 2013-10-10, release date: 2013-11-20, Last modification date: 2024-11-06)

Primary citation

de Vries, R.P.,Zhu, X.,McBride, R.,Rigter, A.,Hanson, A.,Zhong, G.,Hatta, M.,Xu, R.,Yu, W.,Kawaoka, Y.,de Haan, C.A.,Wilson, I.A.,Paulson, J.C.
Hemagglutinin Receptor Specificity and Structural Analyses of Respiratory Droplet-Transmissible H5N1 Viruses.
J.Virol., 88:768-773, 2014

PubMed Abstract: Two ferret-adapted H5N1 viruses capable of respiratory droplet transmission have been reported with mutations in the hemagglutinin receptor-binding site and stalk domains. Glycan microarray analysis reveals that both viruses exhibit a strong shift toward binding to "human-type" α2-6 sialosides but with notable differences in fine specificity. Crystal structure analysis further shows that the stalk mutation causes no obvious perturbation of the receptor-binding pocket, consistent with its impact on hemagglutinin stability without affecting receptor specificity.

PubMed: 24173215
DOI: 10.1128/JVI.02690-13

Experimental method

X-RAY DIFFRACTION (2.9537 Å)