2ht7: Difference between revisions

Revision as of 16:13, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ht7.png

Template:STRUCTURE 2ht7

N8 neuraminidase in open complex with oseltamivirN8 neuraminidase in open complex with oseltamivir

Template:ABSTRACT PUBMED 16915235

About this StructureAbout this Structure

2HT7 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

Page seeded by OCA on Tue Jul 29 16:13:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''N8 neuraminidase in open complex with oseltamivir'''
+===N8 neuraminidase in open complex with oseltamivir===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16915235}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16915235 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16915235}}
 ==About this Structure==
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 [[Category: Neuraminidase]]
 [[Category: Oseltamivir]]
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