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Volumn 84, Issue 2, 2010, Pages 1089-1096

Structure of the nucleoprotein binding domain of Mokola virus phosphoprotein

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOPROTEIN; PHOSPHOPROTEIN;

EID: 73849135618     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01520-09     Document Type: Article
Times cited : (26)

References (48)
  • 5
    • 63149095444 scopus 로고    scopus 로고
    • Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR
    • Bernard, C., S. Gely, J. M. Bourhis, X. Morelli, S. Longhi, and H. Darbon. 2009. Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR. FEBS Lett. 583:1084-1089.
    • (2009) FEBS Lett , vol.583 , pp. 1084-1089
    • Bernard, C.1    Gely, S.2    Bourhis, J.M.3    Morelli, X.4    Longhi, S.5    Darbon, H.6
  • 7
    • 0028117909 scopus 로고
    • In vivo interaction of rabies virus phosphoprotein (P) and nucleoprotein (N): Existence of two N-binding sites on P protein
    • Chenik, M., K. Chebli, Y. Gaudin, and D. Blondel. 1994. In vivo interaction of rabies virus phosphoprotein (P) and nucleoprotein (N): existence of two N-binding sites on P protein. J. Gen. Virol. 75:2889-2896.
    • (1994) J. Gen. Virol , vol.75 , pp. 2889-2896
    • Chenik, M.1    Chebli, K.2    Gaudin, Y.3    Blondel, D.4
  • 8
    • 2642563538 scopus 로고    scopus 로고
    • Phosphorylation of vesicular stomatitis virus phosphoprotein P is indispensable for virus growth
    • Das, S. C., and A. K. Pattnaik. 2004. Phosphorylation of vesicular stomatitis virus phosphoprotein P is indispensable for virus growth. J. Virol. 78:6420-6430.
    • (2004) J. Virol , vol.78 , pp. 6420-6430
    • Das, S.C.1    Pattnaik, A.K.2
  • 10
    • 33644774586 scopus 로고    scopus 로고
    • Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus
    • Ding, H., T. J. Green, S. Lu, and M. Luo. 2006. Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus. J. Virol. 80:2808-2814.
    • (2006) J. Virol , vol.80 , pp. 2808-2814
    • Ding, H.1    Green, T.J.2    Lu, S.3    Luo, M.4
  • 11
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T. J., J. E. Nielsen, J. A. McCammon, and N. A. Baker. 2004. PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32:W665-W667.
    • (2004) Nucleic Acids Res , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 12
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar, R. C. 2004. MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5:113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 13
    • 21344473205 scopus 로고    scopus 로고
    • Replication strategies of rabies virus
    • Finke, S., and K. K. Conzelmann. 2005. Replication strategies of rabies virus. Virus Res. 111:120-131.
    • (2005) Virus Res , vol.111 , pp. 120-131
    • Finke, S.1    Conzelmann, K.K.2
  • 14
    • 0028268671 scopus 로고
    • Both the N- and the C-terminal domains of the nominal phosphoprotein of rabies virus are involved in binding to the nucleoprotein
    • Fu, Z. F., Y. Zheng, W. H. Wunner, H. Koprowski, and B. Dietzschold. 1994. Both the N- and the C-terminal domains of the nominal phosphoprotein of rabies virus are involved in binding to the nucleoprotein. Virology 200:590-597.
    • (1994) Virology , vol.200 , pp. 590-597
    • Fu, Z.F.1    Zheng, Y.2    Wunner, W.H.3    Koprowski, H.4    Dietzschold, B.5
  • 17
    • 58149242876 scopus 로고    scopus 로고
    • Graham, S. C., R. Assenberg, O. Delmas, A. Verma, A. Gholami, C. Talbi, R. J. Owens, D. I. Stuart, J. M. Grimes, and H. Bourhy. 2008. Rhabdovirus matrix protein structures reveal a novel mode of self-association. PLoS Pathog. 4:e1000251.
    • Graham, S. C., R. Assenberg, O. Delmas, A. Verma, A. Gholami, C. Talbi, R. J. Owens, D. I. Stuart, J. M. Grimes, and H. Bourhy. 2008. Rhabdovirus matrix protein structures reveal a novel mode of self-association. PLoS Pathog. 4:e1000251.
  • 18
    • 67650872991 scopus 로고    scopus 로고
    • Green, T. J., and M. Luo. 2009. Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P. Proc. Natl. Acad. Sci. U. S. A. 106:11713-11718.
    • Green, T. J., and M. Luo. 2009. Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P. Proc. Natl. Acad. Sci. U. S. A. 106:11713-11718.
  • 19
    • 33746516378 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleoprotein-RNA complex
    • Green, T. J., X. Zhang, G. W. Wertz, and M. Luo. 2006. Structure of the vesicular stomatitis virus nucleoprotein-RNA complex. Science 313:357-360.
    • (2006) Science , vol.313 , pp. 357-360
    • Green, T.J.1    Zhang, X.2    Wertz, G.W.3    Luo, M.4
  • 20
    • 0033986999 scopus 로고    scopus 로고
    • The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C
    • Gupta, A. K., D. Blondel, S. Choudhary, and A. K. Banerjee. 2000. The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C. J. Virol. 74:91-98.
    • (2000) J. Virol , vol.74 , pp. 91-98
    • Gupta, A.K.1    Blondel, D.2    Choudhary, S.3    Banerjee, A.K.4
  • 21
    • 34250849555 scopus 로고    scopus 로고
    • Interaction of the C-terminal domains of Sendai virus N and P proteins: Comparison of polymerase-nucleocapsid interactions within the paramyxovirus family
    • Houben, K., D. Marion, N. Tarbouriech, R. W. Ruigrok, and L. Blanchard. 2007. Interaction of the C-terminal domains of Sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family. J. Virol. 81:6807-6816.
    • (2007) J. Virol , vol.81 , pp. 6807-6816
    • Houben, K.1    Marion, D.2    Tarbouriech, N.3    Ruigrok, R.W.4    Blanchard, L.5
  • 22
    • 0032425151 scopus 로고    scopus 로고
    • Characterization of rabies virus nucleocapsids and recombinant nucleocapsid-like structures
    • Iseni, F., A. Barge, F. Baudin, D. Blondel, and R. W. Ruigrok. 1998. Characterization of rabies virus nucleocapsids and recombinant nucleocapsid-like structures. J. Gen. Virol. 79:2909-2919.
    • (1998) J. Gen. Virol , vol.79 , pp. 2909-2919
    • Iseni, F.1    Barge, A.2    Baudin, F.3    Blondel, D.4    Ruigrok, R.W.5
  • 23
    • 0034811975 scopus 로고    scopus 로고
    • Functional interaction map of lyssavirus phosphoprotein: Identification of the minimal transcription domains
    • Jacob, Y., E. Real, and N. Tordo. 2001. Functional interaction map of lyssavirus phosphoprotein: identification of the minimal transcription domains. J. Virol. 75:9613-9622.
    • (2001) J. Virol , vol.75 , pp. 9613-9622
    • Jacob, Y.1    Real, E.2    Tordo, N.3
  • 24
    • 0242582329 scopus 로고    scopus 로고
    • Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein
    • Johansson, K., J. M. Bourhis, V. Campanacci, C. Cambillau, B. Canard, and S. Longhi. 2003. Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. J. Biol. Chem. 278:44567-44573.
    • (2003) J. Biol. Chem , vol.278 , pp. 44567-44573
    • Johansson, K.1    Bourhis, J.M.2    Campanacci, V.3    Cambillau, C.4    Canard, B.5    Longhi, S.6
  • 27
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and K. Henrick. 2007. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372:774-797.
    • (2007) J. Mol. Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 28
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski, R. A., D. S. Moss, and J. M. Thornton. 1993. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231:1049-1067.
    • (1993) J. Mol. Biol , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 29
    • 9944259465 scopus 로고    scopus 로고
    • Interactions amongst rabies virus nucleoprotein, phosphoprotein and genomic RNA in virus-infected and transfected cells
    • Liu, P., J. Yang, X. Wu, and Z. F. Fu. 2004. Interactions amongst rabies virus nucleoprotein, phosphoprotein and genomic RNA in virus-infected and transfected cells. J. Gen. Virol. 85:3725-3734.
    • (2004) J. Gen. Virol , vol.85 , pp. 3725-3734
    • Liu, P.1    Yang, J.2    Wu, X.3    Fu, Z.F.4
  • 30
    • 5144222412 scopus 로고    scopus 로고
    • Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus
    • Mavrakis, M., A. A. McCarthy, S. Roche, D. Blondel, and R. W. Ruigrok. 2004. Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus. J. Mol. Biol. 343:819-831.
    • (2004) J. Mol. Biol , vol.343 , pp. 819-831
    • Mavrakis, M.1    McCarthy, A.A.2    Roche, S.3    Blondel, D.4    Ruigrok, R.W.5
  • 31
    • 33646861788 scopus 로고    scopus 로고
    • Rabies virus chaperone: Identification of the phosphoprotein peptide that keeps nucleoprotein soluble and free from non-specific RNA
    • Mavrakis, M., S. Mehouas, E. Real, F. Iseni, D. Blondel, N. Tordo, and R. W. Ruigrok. 2006. Rabies virus chaperone: identification of the phosphoprotein peptide that keeps nucleoprotein soluble and free from non-specific RNA. Virology 349:422-429.
    • (2006) Virology , vol.349 , pp. 422-429
    • Mavrakis, M.1    Mehouas, S.2    Real, E.3    Iseni, F.4    Blondel, D.5    Tordo, N.6    Ruigrok, R.W.7
  • 33
    • 47749090176 scopus 로고    scopus 로고
    • Formation of guanosine(5′)tetraphospho( 5′)adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus
    • Ogino, T., and A. K. Banerjee. 2008. Formation of guanosine(5′)tetraphospho( 5′)adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus. J. Virol. 82:7729-7734.
    • (2008) J. Virol , vol.82 , pp. 7729-7734
    • Ogino, T.1    Banerjee, A.K.2
  • 34
    • 15244339820 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the rabies virus P protein requires a nuclear localization signal and a CRM1-dependent nuclear export signal
    • Pasdeloup, D., N. Poisson, H. Raux, Y. Gaudin, R. W. Ruigrok, and D. Blondel. 2005. Nucleocytoplasmic shuttling of the rabies virus P protein requires a nuclear localization signal and a CRM1-dependent nuclear export signal. Virology 334:284-293.
    • (2005) Virology , vol.334 , pp. 284-293
    • Pasdeloup, D.1    Poisson, N.2    Raux, H.3    Gaudin, Y.4    Ruigrok, R.W.5    Blondel, D.6
  • 38
    • 0034749347 scopus 로고    scopus 로고
    • Structure of recombinant rabies virus nucleoprotein-RNA complex and identification of the phosphoprotein binding site
    • Schoehn, G., F. Iseni, M. Mavrakis, D. Blondel, and R. W. Ruigrok. 2001. Structure of recombinant rabies virus nucleoprotein-RNA complex and identification of the phosphoprotein binding site. J. Virol. 75:490-498.
    • (2001) J. Virol , vol.75 , pp. 490-498
    • Schoehn, G.1    Iseni, F.2    Mavrakis, M.3    Blondel, D.4    Ruigrok, R.W.5
  • 39
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart, M. 2007. Molecular mechanism of the nuclear protein import cycle. Nat. Rev. Mol. Cell Biol. 8:195-208.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 195-208
    • Stewart, M.1
  • 40
    • 0018792428 scopus 로고
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A
    • Stuart, D. I., M. Levine, H. Muirhead, and D. K. Stammers. 1979. Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A. J. Mol. Biol. 134:109-142.
    • (1979) J. Mol. Biol , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4
  • 41
    • 0029072376 scopus 로고
    • Efficient interaction of the vesicular stomatitis virus P protein with the L protein or the N protein in cells expressing the recombinant proteins
    • Takacs, A. M., and A. K. Banerjee. 1995. Efficient interaction of the vesicular stomatitis virus P protein with the L protein or the N protein in cells expressing the recombinant proteins. Virology 208:821-826.
    • (1995) Virology , vol.208 , pp. 821-826
    • Takacs, A.M.1    Banerjee, A.K.2
  • 42
    • 0027505069 scopus 로고
    • Mapping of interacting domains between the nucleocapsid protein and the phosphoprotein of vesicular stomatitis virus by using a two-hybrid system
    • Takacs, A. M., T. Das, and A. K. Banerjee. 1993. Mapping of interacting domains between the nucleocapsid protein and the phosphoprotein of vesicular stomatitis virus by using a two-hybrid system. Proc. Natl. Acad. Sci. U. S. A. 90:10375-10379.
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , pp. 10375-10379
    • Takacs, A.M.1    Das, T.2    Banerjee, A.K.3
  • 43
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL-X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 44
    • 0027198493 scopus 로고
    • Structure and expression in baculovirus of the Mokola virus glycoprotein: An efficient recombinant vaccine
    • Tordo, N., H. Bourhy, S. Sather, and R. Ollo. 1993. Structure and expression in baculovirus of the Mokola virus glycoprotein: an efficient recombinant vaccine. Virology 194:59-69.
    • (1993) Virology , vol.194 , pp. 59-69
    • Tordo, N.1    Bourhy, H.2    Sather, S.3    Ollo, R.4
  • 45
    • 2442662593 scopus 로고    scopus 로고
    • Association of rabies virus nominal phosphoprotein (P) with viral nucleocapsid (NC) is enhanced by phosphorylation of the viral nucleoprotein (N)
    • Toriumi, H., and A. Kawai. 2004. Association of rabies virus nominal phosphoprotein (P) with viral nucleocapsid (NC) is enhanced by phosphorylation of the viral nucleoprotein (N). Microbiol. Immunol. 48:399-409.
    • (2004) Microbiol. Immunol , vol.48 , pp. 399-409
    • Toriumi, H.1    Kawai, A.2
  • 46
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., and A. Teplyakov. 1997. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30:1022-1025.
    • (1997) J. Appl. Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 47
    • 0034854563 scopus 로고    scopus 로고
    • High-throughput yeast two-hybrid assays for large-scale protein interaction mapping
    • Walhout, A. J., and M. Vidal. 2001. High-throughput yeast two-hybrid assays for large-scale protein interaction mapping. Methods 24:297-306.
    • (2001) Methods , vol.24 , pp. 297-306
    • Walhout, A.J.1    Vidal, M.2


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