1dxp: Difference between revisions

Revision as of 23:46, 30 June 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:1dxp.png

Template:STRUCTURE 1dxp

INHIBITION OF THE HEPATITIS C VIRUS NS3/4A PROTEASE. THE CRYSTAL STRUCTURES OF TWO PROTEASE-INHIBITOR COMPLEXES (APO STRUCTURE)INHIBITION OF THE HEPATITIS C VIRUS NS3/4A PROTEASE. THE CRYSTAL STRUCTURES OF TWO PROTEASE-INHIBITOR COMPLEXES (APO STRUCTURE)

Template:ABSTRACT PUBMED 10702283

About this StructureAbout this Structure

1DXP is a Protein complex structure of sequences from Hepatitis c virus and Hepatitis c virus genotype 1a (isolate 1). Full crystallographic information is available from OCA.

ReferenceReference

Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes., Di Marco S, Rizzi M, Volpari C, Walsh MA, Narjes F, Colarusso S, De Francesco R, Matassa VG, Sollazzo M, J Biol Chem. 2000 Mar 10;275(10):7152-7. PMID:10702283

Page seeded by OCA on Mon Jun 30 23:46:29 2008

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OCA

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-'''INHIBITION OF THE HEPATITIS C VIRUS NS3/4A PROTEASE. THE CRYSTAL STRUCTURES OF TWO PROTEASE-INHIBITOR COMPLEXES (APO STRUCTURE)'''
+===INHIBITION OF THE HEPATITIS C VIRUS NS3/4A PROTEASE. THE CRYSTAL STRUCTURES OF TWO PROTEASE-INHIBITOR COMPLEXES (APO STRUCTURE)===
-==Overview==
+<!--
-The hepatitis C virus NS3 protein contains a serine protease domain with a chymotrypsin-like fold, which is a target for development of therapeutics. We report the crystal structures of this domain complexed with NS4A cofactor and with two potent, reversible covalent inhibitors spanning the P1-P4 residues. Both inhibitors bind in an extended backbone conformation, forming an anti-parallel beta-sheet with one enzyme beta-strand. The P1 residue contributes most to the binding energy, whereas P2-P4 side chains are partially solvent exposed. The structures do not show notable rearrangements of the active site upon inhibitor binding. These results are significant for the development of antivirals.
+The line below this paragraph, {{ABSTRACT_PUBMED_10702283}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10702283 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10702283}}
 ==About this Structure==
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 [[Category: Protease inhibition]]
 [[Category: Serine protease]]
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