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Volumn 86, Issue 12, 2012, Pages 6503-6511

Structure of hepatitis C virus polymerase in complex with primer-template RNA

Author keywords

[No Author keywords available]

Indexed keywords

RNA DIRECTED RNA POLYMERASE; VIRUS ENZYME; VIRUS RNA;

EID: 84864011029     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00386-12     Document Type: Article
Times cited : (104)

References (44)
  • 1
    • 0033571463 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus
    • Ago H, et al. 1999. Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus. Structure 7:1417-1426.
    • (1999) Structure , vol.7 , pp. 1417-1426
    • Ago, H.1
  • 2
    • 23744436747 scopus 로고    scopus 로고
    • Crystal structures of the RNA-dependent RNA polymerase genotype 2a of hepatitis C virus reveal two conformations and suggest mechanisms of inhibition by nonnucleoside inhibitors
    • Biswal BK, et al. 2005. Crystal structures of the RNA-dependent RNA polymerase genotype 2a of hepatitis C virus reveal two conformations and suggest mechanisms of inhibition by nonnucleoside inhibitors. J. Biol. Chem. 280:18202-18210.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18202-18210
    • Biswal, B.K.1
  • 3
    • 0033539482 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus
    • Bressanelli S, et al. 1999. Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus. Proc. Natl. Acad. Sci. U. S. A. 96:13034- 13039.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13034-13039
    • Bressanelli, S.1
  • 5
    • 82555170294 scopus 로고    scopus 로고
    • An objective assessment of conformational variability in complexes of hepatitis C virus polymerase with non-nucleoside inhibitors
    • Caillet-Saguy C, Simister PC, Bressanelli S. 2011. An objective assessment of conformational variability in complexes of hepatitis C virus polymerase with non-nucleoside inhibitors. J. Mol. Biol. 414:370 -384.
    • (2011) J. Mol. Biol. , vol.414 , pp. 370-384
    • Caillet-Saguy, C.1    Simister, P.C.2    Bressanelli, S.3
  • 6
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: all-atom structure validation for macromolecular crystallography
    • Chen VB, et al. 2010. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66:12-21.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 7
    • 1842481188 scopus 로고    scopus 로고
    • The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation
    • Choi KH, et al. 2004. The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation. Proc. Natl. Acad. Sci. U. S. A. 101:4425- 4430.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4425-4430
    • Choi, K.H.1
  • 8
    • 77049121252 scopus 로고    scopus 로고
    • Use of thermal melt curves to assess the quality of enzyme preparations
    • Crowther GJ, et al. 2010. Use of thermal melt curves to assess the quality of enzyme preparations. Anal. Biochem. 399:268 -275.
    • (2010) Anal. Biochem. , vol.399 , pp. 268-275
    • Crowther, G.J.1
  • 10
    • 33845247515 scopus 로고    scopus 로고
    • General catalytic deficiency of hepatitis C virus RNA polymerase with an S282T mutation and mutually exclusive resistance towards 2=-modified nucleotide analogues
    • Dutartre H, Bussetta C, Boretto J, Canard B. 2006. General catalytic deficiency of hepatitis C virus RNA polymerase with an S282T mutation and mutually exclusive resistance towards 2=-modified nucleotide analogues. Antimicrob. Agents Chemother. 50:4161- 4169.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 4161-4169
    • Dutartre, H.1    Bussetta, C.2    Boretto, J.3    Canard, B.4
  • 12
    • 8744222695 scopus 로고    scopus 로고
    • Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a templateprimer RNA
    • Ferrer-Orta C, et al. 2004. Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a templateprimer RNA. J. Biol. Chem. 279:47212- 47221.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47212-47221
    • Ferrer-Orta, C.1
  • 13
    • 77952710653 scopus 로고    scopus 로고
    • Structure of foot-and-mouth disease virus mutant polymerases with reduced sensitivity to ribavirin
    • Ferrer-Orta C, et al. 2010. Structure of foot-and-mouth disease virus mutant polymerases with reduced sensitivity to ribavirin. J. Virol. 84: 6188-6199.
    • (2010) J. Virol. , vol.84 , pp. 6188-6199
    • Ferrer-Orta, C.1
  • 14
    • 79958255214 scopus 로고    scopus 로고
    • Activity and the metabolic activation pathway of the potent and selective hepatitis C virus pronucleotide inhibitor PSI-353661
    • Furman PA, et al. 2011. Activity and the metabolic activation pathway of the potent and selective hepatitis C virus pronucleotide inhibitor PSI-353661. Antiviral Res. 91:120 -132.
    • (2011) Antiviral Res , vol.91 , pp. 120-132
    • Furman, P.A.1
  • 15
    • 78651097570 scopus 로고    scopus 로고
    • Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase
    • Gong P, Peersen OB. 2010. Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 107:22505-22510.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 22505-22510
    • Gong, P.1    Peersen, O.B.2
  • 16
    • 0035919073 scopus 로고    scopus 로고
    • A novel mechanism to ensure terminal initiation by hepatitis C virus NS5B polymerase
    • Hong Z, et al. 2001. A novel mechanism to ensure terminal initiation by hepatitis C virus NS5B polymerase. Virology 285:6 -11.
    • (2001) Virology , vol.285 , pp. 6-11
    • Hong, Z.1
  • 17
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance
    • Huang H, Chopra R, Verdine GL, Harrison SC. 1998. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282:1669 -1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 18
    • 76449099287 scopus 로고    scopus 로고
    • Xds. Acta Crystallogr
    • Kabsch W. 2010. Xds. Acta Crystallogr. D Biol. Crystallogr. 66:125-132.
    • (2010) D Biol. Crystallogr , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 19
    • 81255184396 scopus 로고    scopus 로고
    • Hepatitis C virus nucleotide inhibitors PSI-352938 and PSI-353661 exhibit a novel mechanism of resistance requiring multiple mutations within replicon RNA
    • Lam AM, et al. 2011. Hepatitis C virus nucleotide inhibitors PSI-352938 and PSI-353661 exhibit a novel mechanism of resistance requiring multiple mutations within replicon RNA. J. Virol. 85:12334 -12342.
    • (2011) J. Virol. , vol.85 , pp. 12334-12342
    • Lam, A.M.1
  • 20
    • 59149085501 scopus 로고    scopus 로고
    • The global burden of hepatitis C
    • Lavanchy D. 2009. The global burden of hepatitis C. Liver Int. 29(Suppl. 1):74-81.
    • (2009) Liver Int , vol.29 , Issue.SUPPL. 1 , pp. 74-81
    • Lavanchy, D.1
  • 21
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg CA, et al. 1999. Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nat. Struct. Biol. 6:937-943.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 937-943
    • Lesburg, C.A.1
  • 22
    • 65649112893 scopus 로고    scopus 로고
    • Gene composer: database software for protein construct design, codon engineering, and gene synthesis
    • Lorimer D, et al. 2009. Gene composer: database software for protein construct design, codon engineering, and gene synthesis. BMC Biotechnol. 9:36.
    • (2009) BMC Biotechnol , vol.9 , pp. 36
    • Lorimer, D.1
  • 23
    • 0038467627 scopus 로고    scopus 로고
    • Crystallographic identification of a noncompetitive inhibitor binding site on the hepatitis C virus NS5B RNA polymerase enzyme
    • Love RA, et al. 2003. Crystallographic identification of a noncompetitive inhibitor binding site on the hepatitis C virus NS5B RNA polymerase enzyme. J. Virol. 77:7575-7581.
    • (2003) J. Virol. , vol.77 , pp. 7575-7581
    • Love, R.A.1
  • 24
    • 0033989278 scopus 로고    scopus 로고
    • De novo initiation of RNA synthesis by the RNAdependent RNA polymerase (NS5B) of hepatitis C virus
    • Luo G, et al. 2000. De novo initiation of RNA synthesis by the RNAdependent RNA polymerase (NS5B) of hepatitis C virus. J. Virol. 74:851- 863.
    • (2000) J. Virol. , vol.74 , pp. 851-863
    • Luo, G.1
  • 25
    • 0035824671 scopus 로고    scopus 로고
    • Hepatitis C virus RNA-dependent RNA polymerase (NS5B) as a mediator of the antiviral activity of ribavirin
    • Maag D, Castro C, Hong Z, Cameron CE. 2001. Hepatitis C virus RNA-dependent RNA polymerase (NS5B) as a mediator of the antiviral activity of ribavirin. J. Biol. Chem. 276:46094-46098.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46094-46098
    • Maag, D.1    Castro, C.2    Hong, Z.3    Cameron, C.E.4
  • 26
    • 34249845069 scopus 로고    scopus 로고
    • Crystal structure of the RNA polymerase domain of the West Nile virus non-structural protein 5
    • Malet H, et al. 2007. Crystal structure of the RNA polymerase domain of the West Nile virus non-structural protein 5. J. Biol. Chem. 282:10678- 10689.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10678-10689
    • Malet, H.1
  • 27
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor
    • Matulis D, Kranz JK, Salemme FR, Todd MJ. 2005. Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor. Biochemistry 44:5258 -5266.
    • (2005) Biochemistry , vol.44 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 28
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. 2007. Phaser crystallographic software. J. Appl. Crystallogr. 40:658-674.
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 29
    • 33846589710 scopus 로고    scopus 로고
    • Mechanism of activation of beta-D-2=-deoxy-2=-fluoro-2=-c-methylcytidine and inhibition of hepatitis C virus NS5B RNA polymerase
    • Murakami E, et al. 2007. Mechanism of activation of beta-D-2=-deoxy-2=-fluoro-2=-c-methylcytidine and inhibition of hepatitis C virus NS5B RNA polymerase. Antimicrob. Agents Chemother. 51:503-509.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 503-509
    • Murakami, E.1
  • 31
    • 0037470586 scopus 로고    scopus 로고
    • Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de-novo initiation
    • O'Farrell D, Trowbridge R, Rowlands D, Jager J. 2003. Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de-novo initiation. J. Mol. Biol. 326:1025-1035.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1025-1035
    • O'Farrell, D.1    Trowbridge, R.2    Rowlands, D.3    Jager, J.4
  • 33
    • 20944431615 scopus 로고    scopus 로고
    • Inhibitors of HCV NS5B polymerase Part 1 evaluation of the southern region of (2Z)-2-(benzoylamino)-3-(5-phenyl-2-furyl)acrylic acid
    • Pfefferkorn JA, et al. 2005. Inhibitors of HCV NS5B polymerase. Part 1: evaluation of the southern region of (2Z)-2-(benzoylamino)-3-(5-phenyl-2-furyl)acrylic acid. Bioorg. Med. Chem. Lett. 15:2481-2486.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 2481-2486
    • Pfefferkorn, J.A.1
  • 34
    • 79952170633 scopus 로고    scopus 로고
    • Inhibitors of the hepatitis C virus RNA-dependent RNA polymerase NS5B
    • Powdrill MH, Bernatchez JA, Gotte M. 2010. Inhibitors of the hepatitis C virus RNA-dependent RNA polymerase NS5B. Viruses 2:2169 -2195.
    • (2010) Viruses , vol.2 , pp. 2169-2195
    • Powdrill, M.H.1    Bernatchez, J.A.2    Gotte, M.3
  • 35
    • 65649096202 scopus 로고    scopus 로고
    • Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer
    • Raymond A, et al. 2009. Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer. BMC Biotechnol. 9:37.
    • (2009) BMC Biotechnol , vol.9 , pp. 37
    • Raymond, A.1
  • 36
    • 0035166768 scopus 로고    scopus 로고
    • HCV RNA-dependent RNA polymerase replicates in vitro the 3= terminal region of the minus-strand viral RNA more efficiently than the 3= terminal region of the plus RNA
    • Reigadas S, et al. 2001. HCV RNA-dependent RNA polymerase replicates in vitro the 3= terminal region of the minus-strand viral RNA more efficiently than the 3= terminal region of the plus RNA. Eur. J. Biochem. 268:5857-5867.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5857-5867
    • Reigadas, S.1
  • 37
    • 79952379082 scopus 로고    scopus 로고
    • A comprehensive structure-function comparison of hepatitis C virus strain JFH1 and J6 polymerases reveals a key residue stimulating replication in cell culture across genotypes
    • Schmitt M, et al. 2011. A comprehensive structure-function comparison of hepatitis C virus strain JFH1 and J6 polymerases reveals a key residue stimulating replication in cell culture across genotypes. J. Virol. 85:2565-2581.
    • (2011) J. Virol. , vol.85 , pp. 2565-2581
    • Schmitt, M.1
  • 38
    • 70350309663 scopus 로고    scopus 로고
    • Structural and functional analysis of hepatitis C virus strain JFH1 polymerase
    • Simister P, et al. 2009. Structural and functional analysis of hepatitis C virus strain JFH1 polymerase. J. Virol. 83:11926 -11939.
    • (2009) J. Virol. , vol.83 , pp. 11926-11939
    • Simister, P.1
  • 39
    • 84858722318 scopus 로고    scopus 로고
    • Nucleoside, nucleotide, and non-nucleoside inhibitors of hepatitisCvirus NS5B RNAdependent RNA-polymerase
    • Sofia MJ, Chang W, Furman PA, Mosley RT, Ross BS. 2012. Nucleoside, nucleotide, and non-nucleoside inhibitors of hepatitisCvirus NS5B RNAdependent RNA-polymerase. J. Med. Chem. 55:2481-2531.
    • (2012) J. Med. Chem. , vol.55 , pp. 2481-2531
    • Sofia, M.J.1    Chang, W.2    Furman, P.A.3    Mosley, R.T.4    Ross, B.S.5
  • 40
    • 10744221995 scopus 로고    scopus 로고
    • Mechanism of action and antiviral activity of benzimidazole-based allosteric inhibitors of the hepatitis C virus RNAdependent RNA polymerase
    • Tomei L, et al. 2003. Mechanism of action and antiviral activity of benzimidazole-based allosteric inhibitors of the hepatitis C virus RNAdependent RNA polymerase. J. Virol. 77:13225-13231.
    • (2003) J. Virol. , vol.77 , pp. 13225-13231
    • Tomei, L.1
  • 41
    • 0038322074 scopus 로고    scopus 로고
    • Non- nucleoside analogue inhibitors bind to an allosteric site on HCV NS5B polymerase Crystal structures and mechanism of inhibition
    • Wang M, et al. 2003. Non-nucleoside analogue inhibitors bind to an allosteric site on HCV NS5B polymerase. Crystal structures and mechanism of inhibition. J. Biol. Chem. 278:9489 -9495.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9489-9495
    • Wang, M.1
  • 42
    • 0032546963 scopus 로고    scopus 로고
    • RNA- dependent RNA polymerase activity of the soluble recombinant hepatitis C virus NS5B protein truncated at the Cterminal region
    • Yamashita T, et al. 1998. RNA-dependent RNA polymerase activity of the soluble recombinant hepatitis C virus NS5B protein truncated at the Cterminal region. J. Biol. Chem. 273:15479 -15486.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15479-15486
    • Yamashita, T.1
  • 43
    • 34247610261 scopus 로고    scopus 로고
    • Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1 85-angstrom resolution
    • Yap TL, et al. 2007. Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution. J. Virol. 81:4753- 4765.
    • (2007) J. Virol. , vol.81 , pp. 4753-4765
    • Yap, T.L.1
  • 44
    • 43149087336 scopus 로고    scopus 로고
    • Structural insights into mechanisms of catalysis and inhibition in Norwalk virus polymerase
    • Zamyatkin DF, et al. 2008. Structural insights into mechanisms of catalysis and inhibition in Norwalk virus polymerase. J. Biol. Chem. 283:7705-7712.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7705-7712
    • Zamyatkin, D.F.1


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