1inh: Difference between revisions

Revision as of 13:36, 1 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:1inh.png

Template:STRUCTURE 1inh

INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED WITH AROMATIC BANA111 INHIBITORINFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED WITH AROMATIC BANA111 INHIBITOR

Template:ABSTRACT PUBMED 7650674

About this StructureAbout this Structure

1INH is a Single protein structure of sequence from Influenza a virus subtype n2. Full crystallographic information is available from OCA.

ReferenceReference

Structure-based inhibitors of influenza virus sialidase. A benzoic acid lead with novel interaction., Singh S, Jedrzejas MJ, Air GM, Luo M, Laver WG, Brouillette WJ, J Med Chem. 1995 Aug 18;38(17):3217-25. PMID:7650674

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OCA

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-'''INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED WITH AROMATIC BANA111 INHIBITOR'''
+===INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED WITH AROMATIC BANA111 INHIBITOR===
-==Overview==
+<!--
-Influenza virus sialidase is a surface enzyme that is essential for infection of the virus. The catalytic site is highly conserved among all known influenza variants, suggesting that this protein is a suitable target for drug intervention. The most potent known inhibitors are analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en), particularly the 4-guanidino derivative (4-guanidino-Neu5Ac2en). We utilized the benzene ring of 4-(N-acetylamino)benzoic acids as a cyclic template to substitute for the dihydropyran ring of Neu5Ac2en. In this study several 3-(N-acylamino) derivatives were prepared as potential replacements for the glycerol side chain of Neu5Ac2en, and some were found to interact with the same binding subsite of sialidase. Of greater significance was the observation that the 3-guanidinobenzoic acid derivative (equivalent to the 4-guanidino grouping of 4-guanidino-Neu5Ac2en), the most potent benzoic acid inhibitor of influenza sialidase thus far identified (IC50 = 10 microM), occupied the glycerol-binding subsite on sialidase as opposed to the guanidino-binding subsite. This benzoic acid derivative thus provides a new compound that interacts in a novel manner with the catalytic site of influenza sialidase.
+The line below this paragraph, {{ABSTRACT_PUBMED_7650674}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_7650674}}
 ==About this Structure==
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 [[Category: O-glycosyl]]
 [[Category: Sialidase]]
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