2HTW

N4 neuraminidase in complex with DANA

Summary for 2HTW

• Entry DOI: 10.2210/pdb2htw/pdb
• Related: 2HT5 2HT7 2HT8 2HTQ 2HTR 2HTU 2HTV 2HTY 2HU0 2HU4
• Descriptor: Neuraminidase, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID (2 entities in total)
• Functional Keywords: n4, neuraminidase, dana, hydrolase
• Biological source: Influenza A virus
• Total number of polymer chains: 1
• Total formula weight: 43224.25

Authors

Russell, R.J.,Haire, L.F.,Stevens, D.J.,Collins, P.J.,Lin, Y.P.,Blackburn, G.M.,Hay, A.J.,Gamblin, S.J.,Skehel, J.J. (deposition date: 2006-07-26, release date: 2006-09-05, Last modification date: 2020-07-29)

Primary citation

Russell, R.J.,Haire, L.F.,Stevens, D.J.,Collins, P.J.,Lin, Y.P.,Blackburn, G.M.,Hay, A.J.,Gamblin, S.J.,Skehel, J.J.
The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design.
Nature, 443:45-49, 2006

PubMed Abstract: 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.

PubMed: 16915235
DOI: 10.1038/nature05114

Experimental method

X-RAY DIFFRACTION (3.5 Å)