4n5y

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

Structural highlights

4n5y is a 30 chain structure with sequence from Influenza A virus (A/Viet Nam/1203/2004(H5N1)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.1615Å
Ligands:BMA, MAN, NAG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6DQ33_I04A1 Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324]

Publication Abstract from PubMed

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 towards binding to 'human-type' alpha2-6 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 effecting receptor specificity.

Hemagglutinin receptor specificity and structural analyses of respiratory droplet transmissible H5N1 viruses.,de Vries RP, Zhu X, McBride R, Rigter A, Hanson A, Zhong G, Hatta M, Xu R, Yu W, Kawaoka Y, de Haan CA, Wilson IA, Paulson JC J Virol. 2013 Oct 30. PMID:24173215[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
14 reviews cite this structure
Role of receptor binding specificity in influenza A virus transmission and pathogenesis.
de et al. (2014)
13 more
35 other articles
No citations found

See Also

References

  1. ↑ de Vries RP, Zhu X, McBride R, Rigter A, Hanson A, Zhong G, Hatta M, Xu R, Yu W, Kawaoka Y, de Haan CA, Wilson IA, Paulson JC. Hemagglutinin receptor specificity and structural analyses of respiratory droplet transmissible H5N1 viruses. J Virol. 2013 Oct 30. PMID:24173215 doi:http://dx.doi.org/10.1128/JVI.02690-13

Contents


PDB ID 4n5y

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OCA

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