2ht7

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2ht7, resolution 2.60Å ()
Ligands:
Activity: Exo-alpha-sialidase, with EC number 3.2.1.18
Related: 2ht5, 2ht8
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

N8 neuraminidase in open complex with oseltamivir

Publication Abstract from PubMed

The worldwide spread of H5N1 avian influenza has raised concerns that this virus might acquire the ability to pass readily among humans and cause a pandemic. Two anti-influenza drugs currently being used to treat infected patients are oseltamivir (Tamiflu) and zanamivir (Relenza), both of which target the neuraminidase enzyme of the virus. Reports of the emergence of drug resistance make the development of new anti-influenza molecules a priority. Neuraminidases from influenza type A viruses form two genetically distinct groups: group-1 contains the N1 neuraminidase of the H5N1 avian virus and group-2 contains the N2 and N9 enzymes used for the structure-based design of current drugs. Here we show by X-ray crystallography that these two groups are structurally distinct. Group-1 neuraminidases contain a cavity adjacent to their active sites that closes on ligand binding. Our analysis suggests that it may be possible to exploit the size and location of the group-1 cavity to develop new anti-influenza drugs.

The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design., Russell RJ, Haire LF, Stevens DJ, Collins PJ, Lin YP, Blackburn GM, Hay AJ, Gamblin SJ, Skehel JJ, Nature. 2006 Sep 7;443(7107):45-9. Epub 2006 Aug 16. PMID:16915235

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

About this Structure

2ht7 is a 1 chain structure with sequence from Influenza a virus. Full crystallographic information is available from OCA.

See Also

Reference

  • Russell RJ, Haire LF, Stevens DJ, Collins PJ, Lin YP, Blackburn GM, Hay AJ, Gamblin SJ, Skehel JJ. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature. 2006 Sep 7;443(7107):45-9. Epub 2006 Aug 16. PMID:16915235 doi:http://dx.doi.org/10.1038/nature05114

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