2ht5

OverviewOverview

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.

About this StructureAbout this Structure

2HT5 is a Single protein structure of sequence from Influenza a virus with NDG and CA as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Full crystallographic information is available from OCA.

ReferenceReference

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

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