1A1V
HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA
1A1V の概要
エントリーDOI | 10.2210/pdb1a1v/pdb |
分子名称 | DNA (5'-D(*UP*UP*UP*UP*UP*UP*UP*U)-3'), PROTEIN (NS3 PROTEIN), SULFATE ION, ... (4 entities in total) |
機能のキーワード | hepatitis c virus, rna helicase, nonstructural proteins, single-stranded dna, hydrolase-dna complex, hydrolase/dna |
由来する生物種 | Hepatitis C virus (isolate H) 詳細 |
細胞内の位置 | 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 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 53734.73 |
構造登録者 | Kim, J.L.,Morgenstern, K.A.,Griffith, J.P.,Dwyer, M.D.,Thomson, J.A.,Murcko, M.A.,Lin, C.,Caron, P.R. (登録日: 1997-12-17, 公開日: 1999-01-13, 最終更新日: 2024-10-30) |
主引用文献 | 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 Cited by 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: 9493270DOI: 10.1016/S0969-2126(98)00010-0 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
構造検証レポート
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