1dy9

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Revision as of 11:33, 20 November 2007

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spinqualitylabelsall models 1dy9, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

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.

About this Structure

1DY9 is a Single protein structure of sequence from Viruses with ZN as ligand. Full crystallographic information is available from OCA.

Reference

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

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