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Volumn 12, Issue 8, 2004, Pages 1533-1544

The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: A dual function target for common cold antiviral therapy

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; RNA DIRECTED RNA POLYMERASE; VIRUS PROTEIN;

EID: 4143147318     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.05.024     Document Type: Article
Times cited : (95)

References (49)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams J.P., Leslie A.G.W. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D Biol. Crystallogr. 52:1996;30-42
    • (1996) Acta Crystallogr. D Biol. Crystallogr , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 3
    • 0032549512 scopus 로고    scopus 로고
    • Site size of cooperative single-stranded RNA binding by poliovirus RNA-dependent RNA polymerase
    • Beckman M.T., Kirkegaard K. Site size of cooperative single-stranded RNA binding by poliovirus RNA-dependent RNA polymerase. J. Biol. Chem. 273:1998;6724-6730
    • (1998) J. Biol. Chem. , vol.273 , pp. 6724-6730
    • Beckman, M.T.1    Kirkegaard, K.2
  • 6
    • 0141847908 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol) structure, function, and mechanism
    • B.L. Semler, & E. Wimmer. Washington, DC: ASM Press
    • Cameron C.E., Gohara D.W., Arnold J.J. Poliovirus RNA-dependent RNA polymerase (3Dpol). structure, function, and mechanism Semler B.L., Wimmer E. Molecular Biology of Picornaviruses. 2002;255-267 ASM Press, Washington, DC
    • (2002) Molecular Biology of Picornaviruses , pp. 255-267
    • Cameron, C.E.1    Gohara, D.W.2    Arnold, J.J.3
  • 7
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4) the CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project, Number 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50:1994;760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 8
    • 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 K.H., Groarke J.M., Young D.C., Kuhn R.J., Smith J.L., Pevear D.C., Rossmann M.G. 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. USA. 101:2004;4425-4430
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4425-4430
    • Choi, K.H.1    Groarke, J.M.2    Young, D.C.3    Kuhn, R.J.4    Smith, J.L.5    Pevear, D.C.6    Rossmann, M.G.7
  • 9
    • 0141916528 scopus 로고    scopus 로고
    • Rhinoviruses
    • D.M. Knipe, & P.M. Howley. Philadelphia: Lippincott Williams & Wilkins
    • Couch R.B. Rhinoviruses. Knipe D.M., Howley P.M. Fields Virology. 2001;777-797 Lippincott Williams & Wilkins, Philadelphia
    • (2001) Fields Virology , pp. 777-797
    • Couch, R.B.1
  • 12
    • 0034756387 scopus 로고    scopus 로고
    • Biochemical and genetic studies of the initiation of human rhinovirus 2 RNA replication: Purification and enzymatic analysis of the RNA-dependent RNA polymerase 3D(pol)
    • Gerber K., Wimmer E., Paul A.V. Biochemical and genetic studies of the initiation of human rhinovirus 2 RNA replication. purification and enzymatic analysis of the RNA-dependent RNA polymerase 3D(pol) J. Virol. 75:2001;10969-10978
    • (2001) J. Virol. , vol.75 , pp. 10969-10978
    • Gerber, K.1    Wimmer, E.2    Paul, A.V.3
  • 13
    • 0034682792 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol) structural, biochemical, and biological analysis of conserved structural motifs a and B
    • Gohara D.W., Crotty S., Arnold J.J., Yoder J.D., Andino R., Cameron C.E. Poliovirus RNA-dependent RNA polymerase (3Dpol). structural, biochemical, and biological analysis of conserved structural motifs A and B J. Biol. Chem. 275:2000;25523-25532
    • (2000) J. Biol. Chem. , vol.275 , pp. 25523-25532
    • Gohara, D.W.1    Crotty, S.2    Arnold, J.J.3    Yoder, J.D.4    Andino, R.5    Cameron, C.E.6
  • 18
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen J.L., Long A.M., Schultz S.C. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure. 5:1997;1109-1122
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 21
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug design
    • Huang H., Chopra R., Verdine D.L., Harrison S.C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase. implications for drug design Science. 282:1998;1669-1675
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, D.L.3    Harrison, S.C.4
  • 22
    • 0036842233 scopus 로고    scopus 로고
    • Biochemical characterization of rhinovirus RNA-dependent RNA polymerase
    • Hung M., Gibbs C.S., Tsiang M. Biochemical characterization of rhinovirus RNA-dependent RNA polymerase. Antiviral Res. 56:2002;99-114
    • (2002) Antiviral Res. , vol.56 , pp. 99-114
    • Hung, M.1    Gibbs, C.S.2    Tsiang, M.3
  • 24
    • 0037046546 scopus 로고    scopus 로고
    • Structure-based design of a parallel synthetic array directed toward the discovery of irreversible inhibitors of human rhinovirus 3C protease
    • Johnson T.O., Hua Y., Luu H.T., Brown E.L., Chan F., Chu S.S., Dragovich P.S., Eastman B.W., Ferre R.A., Fuhrman S.A., et al. Structure-based design of a parallel synthetic array directed toward the discovery of irreversible inhibitors of human rhinovirus 3C protease. J. Med. Chem. 45:2002;2016-2023
    • (2002) J. Med. Chem. , vol.45 , pp. 2016-2023
    • Johnson, T.O.1    Hua, Y.2    Luu, H.T.3    Brown, E.L.4    Chan, F.5    Chu, S.S.6    Dragovich, P.S.7    Eastman, B.W.8    Ferre, R.A.9    Fuhrman, S.A.10
  • 26
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and shematic plots of protein structures
    • Kraulis P.J. Molscript. a program to produce both detailed and shematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 27
    • 0028300519 scopus 로고
    • Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate
    • Larsen T.M., Laughlin L.T., Holden H.M., Rayment I., Reed G.H. Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate. Biochemistry. 33:1994;6301-6309
    • (1994) Biochemistry , vol.33 , pp. 6301-6309
    • Larsen, T.M.1    Laughlin, L.T.2    Holden, H.M.3    Rayment, I.4    Reed, G.H.5
  • 29
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg C.A., Cable M.B., Ferrari E., Hong Z., Mannarino A.F., Weber P.C. Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nat. Struct. Biol. 6:1999;937-943
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 937-943
    • Lesburg, C.A.1    Cable, M.B.2    Ferrari, E.3    Hong, Z.4    Mannarino, A.F.5    Weber, P.C.6
  • 30
    • 0038467627 scopus 로고    scopus 로고
    • Crystallographic identification of a noncompetitive inhibitor binding site on the hepatitis C virus NS5B RNA polymerase enzyme
    • Love R.A., Parge H.E., Yu X., Hickey M.J., Diehl W., Gao J., Wriggers H., Ekker A., Wang L., Thomson J.A., et al. Crystallographic identification of a noncompetitive inhibitor binding site on the hepatitis C virus NS5B RNA polymerase enzyme. J. Virol. 77:2003;7575-7581
    • (2003) J. Virol. , vol.77 , pp. 7575-7581
    • Love, R.A.1    Parge, H.E.2    Yu, X.3    Hickey, M.J.4    Diehl, W.5    Gao, J.6    Wriggers, H.7    Ekker, A.8    Wang, L.9    Thomson, J.A.10
  • 31
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • a
    • Lyle J.M., Bullitt E., Bienz K., Kirkegaard K. Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science. 296:2002;2218-2222. a
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 32
    • 0037013317 scopus 로고    scopus 로고
    • Similar structural basis for membrane localization and protein priming by an RNA-dependent RNA polymerase
    • b
    • Lyle J.M., Clewell A., Richmond K., Richards O.C., Hope D.A., Schultz S.C., Kirkegaard K. Similar structural basis for membrane localization and protein priming by an RNA-dependent RNA polymerase. J. Biol. Chem. 277:2002;16324-16331. b
    • (2002) J. Biol. Chem. , vol.277 , pp. 16324-16331
    • Lyle, J.M.1    Clewell, A.2    Richmond, K.3    Richards, O.C.4    Hope, D.A.5    Schultz, S.C.6    Kirkegaard, K.7
  • 33
    • 0031762554 scopus 로고    scopus 로고
    • The rhinovirus type 14 genome contains an internally located RNA structure that is required for viral replication
    • McKnight K.L., Lemon S.M. The rhinovirus type 14 genome contains an internally located RNA structure that is required for viral replication. RNA. 4:1998;1569-1584
    • (1998) RNA , vol.4 , pp. 1569-1584
    • McKnight, K.L.1    Lemon, S.M.2
  • 34
    • 0002705842 scopus 로고
    • XtalView: A visual protein crystallographic system for X11/Xview
    • McRee D.E. XtalView. a visual protein crystallographic system for X11/Xview J. Mol. Graph. 10:1992;44-47
    • (1992) J. Mol. Graph. , vol.10 , pp. 44-47
    • McRee, D.E.1
  • 35
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merrit E.A., Bacon D.J. Raster3D. photorealistic molecular graphics Methods Enzymol. 277:1997;505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 37
    • 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. Substrate complexes of hepatitis C virus RNA polymerase (HC-J4). structural evidence for nucleotide import and de-novo initiation J. Mol. Biol. 326:2003;1025-1035
    • (2003) J. Mol. Biol. , vol.326 , pp. 1025-1035
    • O'Farrell, D.1    Trowbridge, R.2    Rowlands, D.3    Jager, J.4
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing X-ray diffraction data collected in oscillation mode
    • C.W. Jr. Carter, & R.M. Sweet. New York: Academic Press
    • Otwinowski Z., Minor W. Processing X-ray diffraction data collected in oscillation mode. Carter C.W. Jr., Sweet R.M. Methods in Enzymology. 1997;307-326 Academic Press, New York
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0029330222 scopus 로고
    • Functional oligomerization of poliovirus RNA-dependent RNA polymerase
    • Pata J.D., Schultz S.C., Kirkegaard K. Functional oligomerization of poliovirus RNA-dependent RNA polymerase. RNA. 1:1995;466-477
    • (1995) RNA , vol.1 , pp. 466-477
    • Pata, J.D.1    Schultz, S.C.2    Kirkegaard, K.3
  • 40
    • 0037200001 scopus 로고    scopus 로고
    • Structure-function relationships of the RNA-dependent RNA polymerase from poliovirus (3Dpol). A surface of the primary oligomerization domain functions in capsid precursor processing and VPg uridylylation
    • Pathak H.B., Ghosh S.K., Roberts A.W., Sharma S.D., Yoder J.D., Arnold J.J., Gohara D.W., Barton D.J., Paul A.V., Cameron C.E. Structure-function relationships of the RNA-dependent RNA polymerase from poliovirus (3Dpol). A surface of the primary oligomerization domain functions in capsid precursor processing and VPg uridylylation. J. Biol. Chem. 277:2002;31551-31562
    • (2002) J. Biol. Chem. , vol.277 , pp. 31551-31562
    • Pathak, H.B.1    Ghosh, S.K.2    Roberts, A.W.3    Sharma, S.D.4    Yoder, J.D.5    Arnold, J.J.6    Gohara, D.W.7    Barton, D.J.8    Paul, A.V.9    Cameron, C.E.10
  • 42
    • 0032554886 scopus 로고    scopus 로고
    • Protein-primed RNA synthesis by purified poliovirus RNA polymerase
    • Paul A.V., van Boom J.H., Filippov D., Wimmer E. Protein-primed RNA synthesis by purified poliovirus RNA polymerase. Nature. 393:1998;280-284
    • (1998) Nature , vol.393 , pp. 280-284
    • Paul, A.V.1    Van Boom, J.H.2    Filippov, D.3    Wimmer, E.4
  • 43
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • Ponstingl H., Henrick K., Thornton J.M. Discriminating between homodimeric and monomeric proteins in the crystalline state. Proteins. 41:2000;47-57
    • (2000) Proteins , vol.41 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 44
    • 0000095156 scopus 로고    scopus 로고
    • Picornaviridae: The viruses and their replication
    • D.M. Knipe, & P.M. Howley. Philadelphia: Lippincott Williams & Wilkins
    • Racaniello V.R. Picornaviridae. the viruses and their replication Knipe D.M., Howley P.M. Fields Virology. 2001;685-722 Lippincott Williams & Wilkins, Philadelphia
    • (2001) Fields Virology , pp. 685-722
    • Racaniello, V.R.1
  • 45
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 47
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz T.A. DNA polymerases. structural diversity and common mechanisms J. Biol. Chem. 274:1999;17395-17398
    • (1999) J. Biol. Chem. , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 48
    • 0027182377 scopus 로고
    • Dialkylglycine decarboxylase structure: Bifunctional active site and alkali metal sites
    • Toney M.D., Hohenester E., Cowan S.W., Jansonius J.N. Dialkylglycine decarboxylase structure. bifunctional active site and alkali metal sites Science. 261:1993;756-759
    • (1993) Science , vol.261 , pp. 756-759
    • Toney, M.D.1    Hohenester, E.2    Cowan, S.W.3    Jansonius, J.N.4


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