1A1V

HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA

Summary for 1A1V

• Entry DOI: 10.2210/pdb1a1v/pdb
• Descriptor: DNA (5'-D(*UP*UP*UP*UP*UP*UP*UP*U)-3'), PROTEIN (NS3 PROTEIN), SULFATE ION, ... (4 entities in total)
• Functional Keywords: hepatitis c virus, rna helicase, nonstructural proteins, single-stranded dna, hydrolase-dna complex, hydrolase/dna
• Biological source: Hepatitis C virus (isolate H); More
• Cellular location: Core protein p21: Host endoplasmic reticulum membrane ; Single-pass membrane protein . Core protein p19: Virion . Envelope glycoprotein E1: Virion membrane ; Single-pass type I membrane protein . Envelope glycoprotein E2: Virion membrane ; Single-pass type I membrane protein . p7: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Protease NS2-3: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Serine protease NS3: Host endoplasmic reticulum membrane ; Peripheral membrane protein . Non-structural protein 4A: Host endoplasmic reticulum membrane ; Single-pass type I membrane protein . Non-structural protein 4B: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein. RNA-directed RNA polymerase: Host endoplasmic reticulum membrane ; Single-pass type I membrane protein : P27958
• Total number of polymer chains: 2
• Total formula weight: 53734.73

Authors

Kim, J.L.,Morgenstern, K.A.,Griffith, J.P.,Dwyer, M.D.,Thomson, J.A.,Murcko, M.A.,Lin, C.,Caron, P.R. (deposition date: 1997-12-17, release date: 1999-01-13, Last modification date: 2024-10-30)

Primary citation

Kim, J.L.,Morgenstern, K.A.,Griffith, J.P.,Dwyer, M.D.,Thomson, J.A.,Murcko, M.A.,Lin, C.,Caron, P.R.
Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding.
Structure, 6:89-100, 1998

PubMed Abstract: 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.

PubMed: 9493270
DOI: 10.1016/S0969-2126(98)00010-0

Experimental method

X-RAY DIFFRACTION (2.2 Å)