2ht5: Difference between revisions
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[[Image:2ht5.gif|left|200px]] | [[Image:2ht5.gif|left|200px]] | ||
'''N8 Neuraminidase''' | {{Structure | ||
|PDB= 2ht5 |SIZE=350|CAPTION= <scene name='initialview01'>2ht5</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] | |||
|GENE= | |||
}} | |||
'''N8 Neuraminidase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HT5 is a [ | 2HT5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HT5 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16915235 16915235] | ||
[[Category: Exo-alpha-sialidase]] | [[Category: Exo-alpha-sialidase]] | ||
[[Category: Influenza a virus]] | [[Category: Influenza a virus]] | ||
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[[Category: neuraminidase]] | [[Category: neuraminidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:21:15 2008'' | ||
Revision as of 18:21, 20 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Exo-alpha-sialidase, with EC number 3.2.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N8 Neuraminidase
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. 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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