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Volumn 7, Issue 11, 1999, Pages 1417-1426

Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus

Author keywords

HCV; Hepatitis C virus; NS5B; RNA dependent RNA polymerase; X ray crystallography

Indexed keywords

RNA DIRECTED RNA POLYMERASE; VIRUS ENZYME;

EID: 0033571463     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)80031-3     Document Type: Article
Times cited : (402)

References (45)
  • 1
    • 0033060563 scopus 로고    scopus 로고
    • Global surveillance and control of hepatitis C
    • WHO (1999). Global surveillance and control of hepatitis C. J. Viral Hepatitis 6, 35-47.
    • (1999) J. Viral Hepatitis , vol.6 , pp. 35-47
  • 2
    • 2642650337 scopus 로고    scopus 로고
    • Candidate targets for hepatitis C virus-specific antiviral therapy
    • Bartenschlager, R. (1997). Candidate targets for hepatitis C virus-specific antiviral therapy. Intervirology 40, 378-393.
    • (1997) Intervirology , vol.40 , pp. 378-393
    • Bartenschlager, R.1
  • 3
    • 0030592514 scopus 로고    scopus 로고
    • The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
    • Love, R.A., et al., & Hostomska, Z. (1996). The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 18, 331-342.
    • (1996) Cell , vol.18 , pp. 331-342
    • Love, R.A.1    Hostomska, Z.2
  • 4
    • 16044364658 scopus 로고    scopus 로고
    • Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide
    • Kim, J.L., et al., & Thomson, J.A. (1996). Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 18, 343-355.
    • (1996) Cell , vol.18 , pp. 343-355
    • Kim, J.L.1    Thomson, J.A.2
  • 5
    • 0030979410 scopus 로고    scopus 로고
    • Structure of the hepatitis C virus RNA helicase domain
    • Yao, N., et al., & Weber, P.C. (1997). Structure of the hepatitis C virus RNA helicase domain. Nat. Struct. Biol. 6, 463-467.
    • (1997) Nat. Struct. Biol. , vol.6 , pp. 463-467
    • Yao, N.1    Weber, P.C.2
  • 6
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide
    • Kim, J.L., et al., & Caron, P.R. (1998). Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide. Structure 6, 89-100.
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Caron, P.R.2
  • 7
    • 0030051777 scopus 로고    scopus 로고
    • Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus
    • Behrens, S.E., Tomei, L. & De Francesco, R. (1996). Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus. EMBO J. 15, 12-22.
    • (1996) EMBO J. , vol.15 , pp. 12-22
    • Behrens, S.E.1    Tomei, L.2    De Francesco, R.3
  • 8
    • 0029817050 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerase of hepatitis C virus
    • De Francesco, R., et al., & Jiricny, J. (1996). RNA-dependent RNA polymerase of hepatitis C virus. Methods Enzymol. 275, 58-67.
    • (1996) Methods Enzymol. , vol.275 , pp. 58-67
    • De Francesco, R.1    Jiricny, J.2
  • 9
    • 1842289764 scopus 로고    scopus 로고
    • Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity
    • Lohmann, V., Körner, F., Herian, U. & Bartenschlager, R. (1997). Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity. J. Virol. 71, 8416-8428.
    • (1997) J. Virol. , vol.71 , pp. 8416-8428
    • Lohmann, V.1    Körner, F.2    Herian, U.3    Bartenschlager, R.4
  • 10
    • 0032530621 scopus 로고    scopus 로고
    • Biochemical and kinetic analyses of NS5B RNA-dependent RNA polymerase of the hepatitis C virus
    • Lohmann, V., Roos, A., Körner, F., Koch, J.O. & Bartenschlager, R. (1998). Biochemical and kinetic analyses of NS5B RNA-dependent RNA polymerase of the hepatitis C virus. Virology 249, 108-118.
    • (1998) Virology , vol.249 , pp. 108-118
    • Lohmann, V.1    Roos, A.2    Körner, F.3    Koch, J.O.4    Bartenschlager, R.5
  • 11
    • 0033574540 scopus 로고    scopus 로고
    • Selective stimulation of hepatitis C virus and pestivirus NS5B RNA polymerase activity by GTP
    • Lohmann, V., Overton, H. & Bartenschlager, R. (1999). Selective stimulation of hepatitis C virus and pestivirus NS5B RNA polymerase activity by GTP. J. Biol. Chem. 274, 10807-10815.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10807-10815
    • Lohmann, V.1    Overton, H.2    Bartenschlager, R.3
  • 12
    • 0032816079 scopus 로고    scopus 로고
    • A recombinant hepatitis C virus RNA-dependent RNA polymerase capable of copying the full-length viral RNA
    • Oh, J-W., Ito, T. & Lai, M.C. (1999). A recombinant hepatitis C virus RNA-dependent RNA polymerase capable of copying the full-length viral RNA. J. Virol. 73, 7694-7702.
    • (1999) J. Virol. , vol.73 , pp. 7694-7702
    • Oh, J.-W.1    Ito, T.2    Lai, M.C.3
  • 13
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen, J.L.H., Long, A.M. & Schultz, S.C. (1997). Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 5, 1109-1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.H.1    Long, A.M.2    Schultz, S.C.3
  • 14
    • 0031579246 scopus 로고    scopus 로고
    • Hepatitis C virus NS5B protein is a membrane-associated phosphoprotein with a predominantly perinuclear localization
    • Hwang, S.B., Park, K-J., Kim, Y-S., Sung, Y.C. & Lai, M.M.C. (1997). Hepatitis C virus NS5B protein is a membrane-associated phosphoprotein with a predominantly perinuclear localization. Virology 227, 439-446.
    • (1997) Virology , vol.227 , pp. 439-446
    • Hwang, S.B.1    Park, K.-J.2    Kim, Y.-S.3    Sung, Y.C.4    Lai, M.M.C.5
  • 15
    • 0032546963 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerase activity of the soluble recombinant hepatitis C virus NS5B protein truncated at the C-terminal region
    • Yamashita, T., et al., & Murakami, S. (1998). RNA-dependent RNA polymerase activity of the soluble recombinant hepatitis C virus NS5B protein truncated at the C-terminal region. J. Biol. Chem. 273, 15479-15486.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15479-15486
    • Yamashita, T.1    Murakami, S.2
  • 16
    • 0032902564 scopus 로고    scopus 로고
    • Characterization of soluble hepatitis C virus RNA-dependent RNA polymerase in Escherichia coli
    • Ferrari, E., et al., & Hong, Z. (1999). Characterization of soluble hepatitis C virus RNA-dependent RNA polymerase in Escherichia coli. J. Virol. 73, 1649-1654.
    • (1999) J. Virol. , vol.73 , pp. 1649-1654
    • Ferrari, E.1    Hong, Z.2
  • 17
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 19
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.J., Macarthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-290.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-290
    • Laskowski, R.J.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 20
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structure of open and closed form of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I
    • Li, Y., Korolev, S. & Waksman, G. (1998). Crystal structure of open and closed form of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I. EMBO J. 17, 7514-7525.
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 21
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of α pol, a family replication DNA polymerase from bacteriophage RB69
    • Wang, J., Sattar, A.K.M., Wang, C.C., Karam, J.D., Konigsberg, W.H. & Steitz, T.A. (1997). Crystal structure of α pol, a family replication DNA polymerase from bacteriophage RB69. Cell 89, 1087-1099.
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1    Sattar, A.K.M.2    Wang, C.C.3    Karam, J.D.4    Konigsberg, W.H.5    Steitz, T.A.6
  • 22
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structure of human DNA polymerase β complexed with gapped and nicked DNA
    • Sawaya, M.R., Prasad, R., Wilson, S.H., Kraut, J. & Pelletier, H. (1997). Crystal structure of human DNA polymerase β complexed with gapped and nicked DNA. Biochemistry 36, 11205-11215.
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 23
    • 0033529089 scopus 로고    scopus 로고
    • Structure basis for initiation of transcription from an RNA polymerase-promoter complex
    • Cheetham, G.M.T., Jeruzalmi, D. & Steitz, T.A. (1999). Structure basis for initiation of transcription from an RNA polymerase-promoter complex. Nature 399, 80-83.
    • (1999) Nature , vol.399 , pp. 80-83
    • Cheetham, G.M.T.1    Jeruzalmi, D.2    Steitz, T.A.3
  • 24
    • 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, G.L. & Harrison, S.C. (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
  • 25
    • 0031790170 scopus 로고    scopus 로고
    • A novel DNA-binding motif shares structural and repair nucleases and polymerases
    • Yuan, Y-C., Whitson, R.H., Liu, Q., Itakura, K. & Chen, Y. (1998). A novel DNA-binding motif shares structural and repair nucleases and polymerases. Nat. Struct. Biol. 5, 959-964.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 959-964
    • Yuan, Y.-C.1    Whitson, R.H.2    Liu, Q.3    Itakura, K.4    Chen, Y.5
  • 27
    • 0028600673 scopus 로고
    • Substrate specificity of protein kinase CK2
    • Maggio, F., Marin, O. & Pinna, L.A. (1994). Substrate specificity of protein kinase CK2. Cell Biol. Res. 40, 401-409.
    • (1994) Cell Biol. Res. , vol.40 , pp. 401-409
    • Maggio, F.1    Marin, O.2    Pinna, L.A.3
  • 29
    • 0032509209 scopus 로고    scopus 로고
    • Functional analysis of amino acid residues constituting the dNTP binding pocket of HIV-1 reverse transcriptase
    • Harris, D., Kaushik, N., Pandey, P.K., Yadav, P.N.S. & Pandey, V.N. (1998). Functional analysis of amino acid residues constituting the dNTP binding pocket of HIV-1 reverse transcriptase. J. Biol. Chem. 273, 33624-33634.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33624-33634
    • Harris, D.1    Kaushik, N.2    Pandey, P.K.3    Yadav, P.N.S.4    Pandey, V.N.5
  • 30
    • 0031028380 scopus 로고    scopus 로고
    • Conferring RNA polymerase activity to a DNA polymerase: A single residue in reverse transcriptase controls substrate selection
    • Gao, G., et al., & Goff, S.P. (1997). Conferring RNA polymerase activity to a DNA polymerase: A single residue in reverse transcriptase controls substrate selection. Proc. Natl Acad. Sci. USA 94, 407-411.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 407-411
    • Gao, G.1    Goff, S.P.2
  • 31
    • 0032798689 scopus 로고    scopus 로고
    • Specific interaction between the hepatitis C virus NS5B RNA polymerase and the 3′ end of the viral RNA
    • Cheng, J-C., Chang, M-F. & Chang, S.C. (1999). Specific interaction between the hepatitis C virus NS5B RNA polymerase and the 3′ end of the viral RNA. J. Virol. 73, 7044-7049.
    • (1999) J. Virol. , vol.73 , pp. 7044-7049
    • Cheng, J.-C.1    Chang, M.-F.2    Chang, S.C.3
  • 32
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch, O., Sauvaget, I., Delarue. M. & Tordo, N. (1989). Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J. 8, 3867-3874.
    • (1989) EMBO J. , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 33
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and SPI-BLAST: A new generation of protein database search programs
    • Altschul, S.F., et al., & Lipman, D. (1997). Gapped BLAST and SPI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Lipman, D.2
  • 34
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S. & Richardson, C.C. (1985). A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl Acad. Sci. USA 82, 1074-1078.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 35
    • 0002864734 scopus 로고
    • Preparation of selenomethionyl protein crystals
    • (Ducruix, A. & Giegé, R., eds), Oxford University Press, Oxford, UK
    • Doublié S. & Carter, C.W., Jr. (1992). Preparation of selenomethionyl protein crystals. In Crystallization of Nucleic Acids and Proteins: A Practical Approach. (Ducruix, A. & Giegé, R., eds), pp. 311-317, Oxford University Press, Oxford, UK.
    • (1992) Crystallization of Nucleic Acids and Proteins: A Practical Approach , pp. 311-317
    • Doublié, S.1    Carter C.W., Jr.2
  • 36
    • 0000293676 scopus 로고
    • X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation
    • Sakabe, N. (1991). X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instrum. Methods A 303, 448-463.
    • (1991) Nucl. Instrum. Methods A , vol.303 , pp. 448-463
    • Sakabe, N.1
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1
  • 39
    • 0028103275 scopus 로고
    • The CCP4: A suite of programs for protein crystallography
    • Collaborative Computational Project, Number 4. (1994). The CCP4: A suite of programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 40
    • 84943920736 scopus 로고
    • Phase annealing in SHELX-90; direct methods for larger structures
    • Sheldrick, G.M. (1990). Phase annealing in SHELX-90; direct methods for larger structures. Acta Crystallogr. A 46, 467-473.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 467-473
    • Sheldrick, G.M.1
  • 41
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • Fortelle, E.L. & Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • Fortelle, E.L.1    Bricogne, G.2
  • 42
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 43
    • 0000614826 scopus 로고    scopus 로고
    • An algorithm for automatic indexing of oscillation images using fourier analysis
    • Steller, I., Bolotovsky, R. & Rossmann, M. (1997). An algorithm for automatic indexing of oscillation images using fourier analysis. J. Appl. Crystallogr. 30, 1036-1040.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1036-1040
    • Steller, I.1    Bolotovsky, R.2    Rossmann, M.3
  • 44
    • 0001935308 scopus 로고
    • Data collection and processing
    • (Sawyer, L., Isaacs, N. & Bailey, S., eds), SERC Daresbury Laboratory, England
    • Leslie, A.G.W. (1993). Data collection and processing. In Proceedings of the CCP4 Study Weekend. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp 44-51, SERC Daresbury Laboratory, England
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 44-51
    • Leslie, A.G.W.1
  • 45
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structure
    • Koradi, R., Billeter, M. & Wüthrich, K. (1996). MOLMOL: A program for display and analysis of macromolecular structure. J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


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