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Volumn 439, Issue 7072, 2006, Pages 38-44

Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; BIOLOGICAL MEMBRANES; CATALYSIS; CELLS; CONFORMATIONS; CRYSTAL STRUCTURE; GENES; PROTEINS;

EID: 30144436116     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04322     Document Type: Article
Times cited : (359)

References (49)
  • 1
    • 0001178028 scopus 로고    scopus 로고
    • eds Knipe, D. M. & Howley, P. M. Lippincott, Williams and Wilkins, Philadelphia
    • Lamb, R. A. & Kolakofsky, D. in Fields Virology 4th edn (eds Knipe, D. M. & Howley, P. M.) 1305-1340 (Lippincott, Williams and Wilkins, Philadelphia, 2001).
    • (2001) Fields Virology 4th Edn , pp. 1305-1340
    • Lamb, R.A.1    Kolakofsky, D.2
  • 2
    • 0028943779 scopus 로고
    • A morbillivirus that caused fatal disease in horses and humans
    • Murray, K. et al. A morbillivirus that caused fatal disease in horses and humans. Science 268, 94-97 (1995).
    • (1995) Science , vol.268 , pp. 94-97
    • Murray, K.1
  • 3
    • 0034717054 scopus 로고    scopus 로고
    • Nipah virus: A recently emergent deadly paramyxovirus
    • Chua, K. B. et al. Nipah virus: a recently emergent deadly paramyxovirus. Science 288, 1432-1435 (2000).
    • (2000) Science , vol.288 , pp. 1432-1435
    • Chua, K.B.1
  • 4
    • 0027426010 scopus 로고
    • The human CD46 molecule is a receptor for measles virus (Edmonston strain)
    • Dorig, R. E., Marcil, A., Chopra, A. & Richardson, C. D. The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 75, 295-305 (1993).
    • (1993) Cell , vol.75 , pp. 295-305
    • Dorig, R.E.1    Marcil, A.2    Chopra, A.3    Richardson, C.D.4
  • 6
    • 22944445501 scopus 로고    scopus 로고
    • EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus
    • Negrete, O. A. et al. EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus. Nature 436, 401-405 (2005).
    • (2005) Nature , vol.436 , pp. 401-405
    • Negrete, O.A.1
  • 7
    • 23044517161 scopus 로고    scopus 로고
    • Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus
    • Bonaparte, M. I. et al. Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus. Proc. Natl Acad. Sci. USA 102, 10652-10657 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10652-10657
    • Bonaparte, M.I.1
  • 8
    • 0032798395 scopus 로고    scopus 로고
    • Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G
    • Feldman, S. A., Hendry, R. M. & Beeler, J. A. Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G. J. Virol. 73, 6610-6617 (1999).
    • (1999) J. Virol. , vol.73 , pp. 6610-6617
    • Feldman, S.A.1    Hendry, R.M.2    Beeler, J.A.3
  • 9
    • 0027430672 scopus 로고
    • Paramyxovirus fusion: A hypothesis for changes
    • Lamb, R. A. Paramyxovirus fusion: a hypothesis for changes. Virology 197, 1-11 (1993).
    • (1993) Virology , vol.197 , pp. 1-11
    • Lamb, R.A.1
  • 10
    • 0034445297 scopus 로고    scopus 로고
    • Virus membrane fusion proteins: Biological machines that undergo a metamorphosis
    • Dutch, R. E., Jardetzky, T. S. & Lamb, R. A. Virus membrane fusion proteins: biological machines that undergo a metamorphosis. Biosci. Rep. 20, 597-612 (2000).
    • (2000) Biosci. Rep. , vol.20 , pp. 597-612
    • Dutch, R.E.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 12
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J. & Wiley, D. C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69, 531-569 (2000).
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 13
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M. & Kim, P. S. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70, 777-810 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 15
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta, R. A., Wild, C. T., Weng, Y. & Weiss, C. D. Capture of an early fusion-active conformation of HIV-1 gp41. Nature Struct. Biol. 5, 276-279 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 16
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion
    • Russell, C. J., Jardetzky, T. S. & Lamb, R. A. Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion. EMBO J. 20, 4024-4034 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 17
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker, K., Dutch, R. E., Lamb, R. A. & Jardetzky, T. S. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell 3, 309-319 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 18
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B. et al. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151, 413-423 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1
  • 19
    • 0032529672 scopus 로고    scopus 로고
    • A core trimer of the paramyxovirus fusion protein: Parallels to influenza virus hemagglutinin and HIV-1 gp41
    • Joshi, S. B., Dutch, R. E. & Lamb, R. A. A core trimer of the paramyxovirus fusion protein: parallels to influenza virus hemagglutinin and HIV-1 gp41. Virology 248, 20-34 (1998).
    • (1998) Virology , vol.248 , pp. 20-34
    • Joshi, S.B.1    Dutch, R.E.2    Lamb, R.A.3
  • 20
    • 21544470513 scopus 로고    scopus 로고
    • Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein
    • Yin, H. S., Paterson, R. G., Wen, X., Lamb, R. A. & Jardetzky, T. S. Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein. Proc. Natl Acad Sci. USA 102, 9288-9293 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9288-9293
    • Yin, H.S.1    Paterson, R.G.2    Wen, X.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 21
    • 0035083470 scopus 로고    scopus 로고
    • The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion
    • Chen, L. et al. The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion. Structure 9, 255-266 (2001).
    • (2001) Structure , vol.9 , pp. 255-266
    • Chen, L.1
  • 22
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman, P. M. & Lawrence, M. C. The structural biology of type I viral membrane fusion. Nature Rev. Mol. Cell Biol. 4, 309-319 (2003).
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 23
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P. B., Zhang, T., Kim, P. S. & Alber, T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262, 1401-1407 (1993).
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 24
    • 3042550474 scopus 로고    scopus 로고
    • Activation of a paramyxovirus fusion protein is modulated by inside-out signalling from the cytoplasmic tail
    • Waning, D. L., Russell, C. J., Jardetzky, T. S. & Lamb, R. A. Activation of a paramyxovirus fusion protein is modulated by inside-out signalling from the cytoplasmic tail. Proc. Natl Acad. Sci. USA 101, 9217-9222 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9217-9222
    • Waning, D.L.1    Russell, C.J.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 25
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus
    • Stevens, J. Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science 303, 1866-1870 (2004).
    • (2004) Science , vol.303 , pp. 1866-1870
    • Stevens, J.1
  • 26
    • 14244261360 scopus 로고    scopus 로고
    • A chimeric protein of simian immunodeficiency virus envelope glycoprotein gp140 and Escherichia coli aspartate transcarbamoylase
    • Chen, B. et al. A chimeric protein of simian immunodeficiency virus envelope glycoprotein gp140 and Escherichia coli aspartate transcarbamoylase. J. Virol. 78, 4508-4516 (2004).
    • (2004) J. Virol. , vol.78 , pp. 4508-4516
    • Chen, B.1
  • 27
    • 0034004321 scopus 로고    scopus 로고
    • Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution
    • Yang, X. et al. Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution. J. Virol. 74, 4746-4754 (2000).
    • (2000) J. Virol. , vol.74 , pp. 4746-4754
    • Yang, X.1
  • 28
    • 0036231093 scopus 로고    scopus 로고
    • Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin
    • Yang, X. et al. Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin. J. Virol. 76, 4634-4642 (2002).
    • (2002) J. Virol. , vol.76 , pp. 4634-4642
    • Yang, X.1
  • 29
    • 0343618590 scopus 로고    scopus 로고
    • Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that it forms with monoclonal antibodies
    • Calder, L. J. et al. Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that it forms with monoclonal antibodies. Virology 271, 122-131 (2000).
    • (2000) Virology , vol.271 , pp. 122-131
    • Calder, L.J.1
  • 30
    • 0034712879 scopus 로고    scopus 로고
    • Fusion protein of the paramyxovirus SV5: Destabilizing and stabilizing mutants of fusion activation
    • Paterson, R. G., Russell, C. J. & Lamb, R. A. Fusion protein of the paramyxovirus SV5: destabilizing and stabilizing mutants of fusion activation. Virology 270, 17-30 (2000).
    • (2000) Virology , vol.270 , pp. 17-30
    • Paterson, R.G.1    Russell, C.J.2    Lamb, R.A.3
  • 31
    • 0242298583 scopus 로고    scopus 로고
    • A dual-functional paramyxovirus F protein regulatory switch segment: Activation and membrane fusion
    • Russell, C. J., Kantor, K. L., Jardetzky, T. S. & Lamb, R. A. A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusion. J. Cell Biol. 163, 363-374 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 363-374
    • Russell, C.J.1    Kantor, K.L.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 32
    • 10044243988 scopus 로고    scopus 로고
    • Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state
    • Russell, C. J., Jardetzky, T. S. & Lamb, R. A. Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state. J. Virol. 78, 13727-13742 (2004).
    • (2004) J. Virol. , vol.78 , pp. 13727-13742
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 33
    • 0033953651 scopus 로고    scopus 로고
    • An amino acid in the heptad repeat 1 domain is important for the haemagglutinin-neuraminidase-independent fusing activity of simian virus 5 fusion protein
    • Ito, M., Nishio, M., Komada, H., Ito, Y. & Tsurudome, M. An amino acid in the heptad repeat 1 domain is important for the haemagglutinin- neuraminidase-independent fusing activity of simian virus 5 fusion protein. J. Gen. Virol. 81, 719-727 (2000).
    • (2000) J. Gen. Virol. , vol.81 , pp. 719-727
    • Ito, M.1    Nishio, M.2    Komada, H.3    Ito, Y.4    Tsurudome, M.5
  • 34
    • 0034853335 scopus 로고    scopus 로고
    • Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: Difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface
    • Tsurudome, M. et al. Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface. J. Virol. 75, 8999-9009 (2001).
    • (2001) J. Virol. , vol.75 , pp. 8999-9009
    • Tsurudome, M.1
  • 35
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • Gibbons, D. L. et al. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 427, 320-325 (2004).
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1
  • 36
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319 (2004).
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 37
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I. A., Skehel, J. J. & Wiley, D. C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289, 366-375 (1981).
    • (1981) Nature , vol.289 , pp. 366-375
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 38
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J. & Wiley, D. C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43 (1994).
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 39
    • 13844302894 scopus 로고    scopus 로고
    • Structure of an unliganded simian immunodeficiency virus gp120 core
    • Chen, B. et al. Structure of an unliganded simian immunodeficiency virus gp120 core. Nature 433, 834-841 (2005).
    • (2005) Nature , vol.433 , pp. 834-841
    • Chen, B.1
  • 40
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P. D. et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659 (1998).
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1
  • 41
    • 0024512971 scopus 로고
    • Analysis of the relationship between cleavability of a paramyxovirus fusion protein and length of the connecting peptide
    • Paterson, R. G., Shaughnessy, M. A. & Lamb, R. A. Analysis of the relationship between cleavability of a paramyxovirus fusion protein and length of the connecting peptide. J. Virol. 63, 1293-1301 (1989).
    • (1989) J. Virol. , vol.63 , pp. 1293-1301
    • Paterson, R.G.1    Shaughnessy, M.A.2    Lamb, R.A.3
  • 42
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury, P. B., Kim, P. S. & Alber, T. Crystal structure of an isoleucine-zipper trimer. Nature 371, 80-83 (1994).
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4
    • Collaborative Computational Project No. 4, The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 44
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T. C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystallogr. D 55, 849-861 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 47
    • 24044475924 scopus 로고    scopus 로고
    • Phased translation function revisited: Structure solution of the cofilin-homology domain from yeast actin-binding protein 1 using six-dimensional searches
    • Strokopytov, B. V. et al. Phased translation function revisited: structure solution of the cofilin-homology domain from yeast actin-binding protein 1 using six-dimensional searches. Acta Crystallogr. D 61, 285-293 (2005).
    • (2005) Acta Crystallogr. D , vol.61 , pp. 285-293
    • Strokopytov, B.V.1
  • 49
    • 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. 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).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


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