2htw: Difference between revisions
New page: left|200px<br /><applet load="2htw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2htw, resolution 3.5Å" /> '''N4 neuraminidase in c... |
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==Overview== | ==Overview== | ||
The worldwide spread of H5N1 avian influenza has raised concerns that this | 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 Structure== | ==About this Structure== | ||
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[[Category: Influenza a virus]] | [[Category: Influenza a virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Blackburn, G | [[Category: Blackburn, G M.]] | ||
[[Category: Collins, P | [[Category: Collins, P J.]] | ||
[[Category: Gamblin, S | [[Category: Gamblin, S J.]] | ||
[[Category: Haire, L | [[Category: Haire, L F.]] | ||
[[Category: Hay, A | [[Category: Hay, A J.]] | ||
[[Category: Lin, Y | [[Category: Lin, Y P.]] | ||
[[Category: Russell, R | [[Category: Russell, R J.]] | ||
[[Category: Skehel, J | [[Category: Skehel, J J.]] | ||
[[Category: Stevens, D | [[Category: Stevens, D J.]] | ||
[[Category: DAN]] | [[Category: DAN]] | ||
[[Category: dana]] | [[Category: dana]] | ||
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[[Category: neuraminidase]] | [[Category: neuraminidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:45:40 2008'' | ||
Revision as of 18:45, 21 February 2008
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N4 neuraminidase in complex with DANA
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
2HTW is a Single protein structure of sequence from Influenza a virus with as ligand. 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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