2amd: Difference between revisions

Revision as of 16:19, 28 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:2amd.png

Template:STRUCTURE 2amd

Crystal Structure Of SARS_CoV Mpro in Complex with an Inhibitor N9Crystal Structure Of SARS_CoV Mpro in Complex with an Inhibitor N9

Template:ABSTRACT PUBMED 16128623

About this StructureAbout this Structure

2AMD is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.

ReferenceReference

Design of wide-spectrum inhibitors targeting coronavirus main proteases., Yang H, Xie W, Xue X, Yang K, Ma J, Liang W, Zhao Q, Zhou Z, Pei D, Ziebuhr J, Hilgenfeld R, Yuen KY, Wong L, Gao G, Chen S, Chen Z, Ma D, Bartlam M, Rao Z, PLoS Biol. 2005 Oct;3(10):e324. Epub 2005 Sep 6. PMID:16128623

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

OCA

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-'''Crystal Structure Of SARS_CoV Mpro in Complex with an Inhibitor N9'''
+===Crystal Structure Of SARS_CoV Mpro in Complex with an Inhibitor N9===
-==Overview==
+<!--
-The genus Coronavirus contains about 25 species of coronaviruses (CoVs), which are important pathogens causing highly prevalent diseases and often severe or fatal in humans and animals. No licensed specific drugs are available to prevent their infection. Different host receptors for cellular entry, poorly conserved structural proteins (antigens), and the high mutation and recombination rates of CoVs pose a significant problem in the development of wide-spectrum anti-CoV drugs and vaccines. CoV main proteases (M(pro)s), which are key enzymes in viral gene expression and replication, were revealed to share a highly conservative substrate-recognition pocket by comparison of four crystal structures and a homology model representing all three genetic clusters of the genus Coronavirus. This conclusion was further supported by enzyme activity assays. Mechanism-based irreversible inhibitors were designed, based on this conserved structural region, and a uniform inhibition mechanism was elucidated from the structures of Mpro-inhibitor complexes from severe acute respiratory syndrome-CoV and porcine transmissible gastroenteritis virus. A structure-assisted optimization program has yielded compounds with fast in vitro inactivation of multiple CoV M(pro)s, potent antiviral activity, and extremely low cellular toxicity in cell-based assays. Further modification could rapidly lead to the discovery of a single agent with clinical potential against existing and possible future emerging CoV-related diseases.
+The line below this paragraph, {{ABSTRACT_PUBMED_16128623}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Anti-parallel a-helice]]
 [[Category: Anti-parallel b-barrel]]
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