1a1v

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spinqualitylabelsall models 1a1v, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA

Overview

BACKGROUND: Hepatitis C virus (HCV) represents a major health concern as, it is responsible for a significant number of hepatitis cases worldwide., Much research has focused on the replicative enzymes of HCV as possible, targets for more effective therapeutic agents. HCV NS3 helicase may, provide one such suitable target. Helicases are enzymes which can unwind, double-stranded regions of DNA or RNA in an ATP-dependent reaction. The, structures of several helicases have been published but the structural, details as to how ATP binding and hydrolysis are coupled to RNA unwinding, are unknown. RESULTS: The structure of the HCV NS3 RNA helicase domain, complexed with a single-stranded DNA oligonucleotide has been solved to, 2.2 A resolution. The protein consists of three structural domains with, the oligonucleotide lying in a groove between the first two domains and, the third. The first two domains have an adenylate kinase like fold, including a phosphate-binding loop in the first domain. CONCLUSIONS: HCV, NS3 helicase is a member of a superfamily of helicases, termed superfamily, II. Residues of NS3 helicase which are conserved among superfamily II, helicases line an interdomain cleft between the first two domains. The, oligonucleotide binds in an orthogonal binding site and contacts, relatively few conserved residues. There are no strong sequence-specific, interactions with the oligonucleotide bases.

About this Structure

1A1V is a Single protein structure of sequence from Hepatitis c virus genotype 1a (isolate h) with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding., Kim JL, Morgenstern KA, Griffith JP, Dwyer MD, Thomson JA, Murcko MA, Lin C, Caron PR, Structure. 1998 Jan 15;6(1):89-100. PMID:9493270

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