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2HTR

N8 neuraminidase in complex with DANA

Summary for 2HTR
Entry DOI10.2210/pdb2htr/pdb
Related2HT5 2HT7 2HT8 2HTQ 2HTU 2HTV 2HTW 2HTY 2HU0 2HU4
DescriptorNeuraminidase, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID (2 entities in total)
Functional Keywordsn8, neuraminidase, dana, hydrolase
Biological sourceInfluenza A virus
Cellular locationVirion membrane (By similarity): Q07599
Total number of polymer chains1
Total formula weight43448.77
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 citationRussell, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

226707

數據於2024-10-30公開中

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