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Volumn 348, Issue 3, 2006, Pages 916-922

Structural characterization of Mumps virus fusion protein core

Author keywords

Crystal structure; Fusion core; Fusion protein; Heptad repeat domains; Mumps virus

Indexed keywords

VIRUS FUSION PROTEIN;

EID: 33747191789     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.07.168     Document Type: Article
Times cited : (13)

References (35)
  • 2
    • 0026552946 scopus 로고
    • Expression of Mumps virus glycoproteins in mammalian cells from cloned cDNAs: both F and HN proteins are required for cell fusion
    • Tanabayashi K., Takeuchi K., Okazaki K., Hishiyama M., and Yamada A. Expression of Mumps virus glycoproteins in mammalian cells from cloned cDNAs: both F and HN proteins are required for cell fusion. Virology 187 (1992) 801-804
    • (1992) Virology , vol.187 , pp. 801-804
    • Tanabayashi, K.1    Takeuchi, K.2    Okazaki, K.3    Hishiyama, M.4    Yamada, A.5
  • 4
    • 0034445297 scopus 로고    scopus 로고
    • Virus membrane fusion proteins: biological machines that undergo a metamorphosis
    • Dutch R.E., Jardetzky T.S., and Lamb R.A. Virus membrane fusion proteins: biological machines that undergo a metamorphosis. Biosci. Rep. 20 (2000) 597-612
    • (2000) Biosci. Rep. , vol.20 , pp. 597-612
    • Dutch, R.E.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 5
    • 0020966928 scopus 로고
    • Biosynthesis of mumps virus F glycoprotein: non-fusing strains efficiently cleave the F glycoprotein precursor
    • Merz D.C., Server A.C., Waxham M.N., and Wolinsky J.S. Biosynthesis of mumps virus F glycoprotein: non-fusing strains efficiently cleave the F glycoprotein precursor. J. Gen. Virol. 64 Pt 7 (1983) 1457-1467
    • (1983) J. Gen. Virol. , vol.64 , Issue.PART 7 , pp. 1457-1467
    • Merz, D.C.1    Server, A.C.2    Waxham, M.N.3    Wolinsky, J.S.4
  • 6
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough P.A., Hughson F.M., Skehel J.J., and Wiley D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371 (1994) 37-43
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 7
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M., Blacklow S.C., and Kim P.S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2 (1995) 1075-1082
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 9
    • 0028864614 scopus 로고
    • A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein
    • Blacklow S.C., Lu M., and Kim P.S. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry 34 (1995) 14955-14962
    • (1995) Biochemistry , vol.34 , pp. 14955-14962
    • Blacklow, S.C.1    Lu, M.2    Kim, P.S.3
  • 10
    • 0029878665 scopus 로고    scopus 로고
    • The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide
    • Weissenhorn W., Wharton S.A., Calder L.J., Earl P.L., Moss B., Aliprandis E., Skehel J.J., and Wiley D.C. The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide. Embo. J. 15 (1996) 1507-1514
    • (1996) Embo. J. , vol.15 , pp. 1507-1514
    • Weissenhorn, W.1    Wharton, S.A.2    Calder, L.J.3    Earl, P.L.4    Moss, B.5    Aliprandis, E.6    Skehel, J.J.7    Wiley, D.C.8
  • 11
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D.C., Fass D., Berger J.M., and Kim P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89 (1997) 263-273
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 12
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K., Liu J., Wang J., Shen S., and Lu M. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 94 (1997) 12303-12308
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 14
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn W., Carfi A., Lee K.H., Skehel J.J., and Wiley D.C. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell 2 (1998) 605-616
    • (1998) Mol. Cell , vol.2 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 15
    • 0032568634 scopus 로고    scopus 로고
    • The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil
    • Weissenhorn W., Calder L.J., Wharton S.A., Skehel J.J., and Wiley D.C. The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil. Proc. Natl. Acad. Sci. USA 95 (1998) 6032-6036
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6032-6036
    • Weissenhorn, W.1    Calder, L.J.2    Wharton, S.A.3    Skehel, J.J.4    Wiley, D.C.5
  • 16
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker K.A., Dutch R.E., Lamb R.A., and Jardetzky T.S. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell 3 (1999) 309-319
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 17
    • 3142663245 scopus 로고    scopus 로고
    • Structural Basis for Coronavirus-mediated membrane fusion: crystal structure of mouse hepatitis virus spike protein fusion core
    • Xu Y., Liu Y., Lou Z., Qin L., Li X., Bai Z., Pang H., Tien P., Gao G.F., and Rao Z. Structural Basis for Coronavirus-mediated membrane fusion: crystal structure of mouse hepatitis virus spike protein fusion core. J. Biol. Chem. 279 (2004) 30514-30522
    • (2004) J. Biol. Chem. , vol.279 , pp. 30514-30522
    • Xu, Y.1    Liu, Y.2    Lou, Z.3    Qin, L.4    Li, X.5    Bai, Z.6    Pang, H.7    Tien, P.8    Gao, G.F.9    Rao, Z.10
  • 18
    • 0031240001 scopus 로고    scopus 로고
    • Enveloped viruses: a common mode of membrane fusion?
    • Hughson F.M. Enveloped viruses: a common mode of membrane fusion?. Curr. Biol. 7 (1997) R565-R569
    • (1997) Curr. Biol. , vol.7
    • Hughson, F.M.1
  • 19
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan D.C., and Kim P.S. HIV entry and its inhibition. Cell 93 (1998) 681-684
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 20
    • 0346848907 scopus 로고    scopus 로고
    • Six-helix bundle assembly and analysis of the central core of mumps virus fusion protein
    • Liu Y., Zhu J., Feng M.G., Tien P., and Gao G.F. Six-helix bundle assembly and analysis of the central core of mumps virus fusion protein. Arch. Biochem. Biophys. 421 (2004) 143-148
    • (2004) Arch. Biochem. Biophys. , vol.421 , pp. 143-148
    • Liu, Y.1    Zhu, J.2    Feng, M.G.3    Tien, P.4    Gao, G.F.5
  • 22
    • 2442705099 scopus 로고    scopus 로고
    • Following the rule: formation of the six-helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors
    • Zhu J., Xiao G., Xu Y., Yuan F., Zheng C., Liu Y., Yan H., Cole D.K., Bell J.I., Rao Z., Tien P., and Gao G.F. Following the rule: formation of the six-helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors. Biochem. Biophys. Res. Commun. 319 (2004) 283-288
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 283-288
    • Zhu, J.1    Xiao, G.2    Xu, Y.3    Yuan, F.4    Zheng, C.5    Liu, Y.6    Yan, H.7    Cole, D.K.8    Bell, J.I.9    Rao, Z.10    Tien, P.11    Gao, G.F.12
  • 23
    • 0038111976 scopus 로고    scopus 로고
    • Design and analysis of post-fusion six-helix bundle of heptad repeat regions from Newcastle disease virus F protein
    • Zhu J., Li P., Wu T., Gao F., Ding Y., Zhang C.W., Rao Z., Gao G.F., and Tien P. Design and analysis of post-fusion six-helix bundle of heptad repeat regions from Newcastle disease virus F protein. Protein Eng. 16 (2003) 373-379
    • (2003) Protein Eng. , vol.16 , pp. 373-379
    • Zhu, J.1    Li, P.2    Wu, T.3    Gao, F.4    Ding, Y.5    Zhang, C.W.6    Rao, Z.7    Gao, G.F.8    Tien, P.9
  • 24
    • 0036190641 scopus 로고    scopus 로고
    • Six-helix bundle assembly and characterization of heptad repeat regions from the F protein of Newcastle disease virus
    • Yu M., Wang E., Liu Y., Cao D., Jin N., Zhang C.W., Bartlam M., Rao Z., Tien P., and Gao G.F. Six-helix bundle assembly and characterization of heptad repeat regions from the F protein of Newcastle disease virus. J. Gen. Virol. 83 (2002) 623-629
    • (2002) J. Gen. Virol. , vol.83 , pp. 623-629
    • Yu, M.1    Wang, E.2    Liu, Y.3    Cao, D.4    Jin, N.5    Zhang, C.W.6    Bartlam, M.7    Rao, Z.8    Tien, P.9    Gao, G.F.10
  • 25
    • 1242340426 scopus 로고    scopus 로고
    • Basis for fusion inhibition by peptides: analysis of the heptad repeat regions of the fusion proteins from Nipah and Hendra viruses, newly emergent zoonotic paramyxoviruses
    • Xu Y., Gao S., Cole D.K., Zhu J., Su N., Wang H., Gao G.F., and Rao Z. Basis for fusion inhibition by peptides: analysis of the heptad repeat regions of the fusion proteins from Nipah and Hendra viruses, newly emergent zoonotic paramyxoviruses. Biochem. Biophys. Res. Commun. 315 (2004) 664-670
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 664-670
    • Xu, Y.1    Gao, S.2    Cole, D.K.3    Zhu, J.4    Su, N.5    Wang, H.6    Gao, G.F.7    Rao, Z.8
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Macromolecular Crystallography, part A (Academic Press,1997)
    • Otwinowski Z., and Minor W. Macromolecular Crystallography, part A (Academic Press,1997). Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 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., and Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta. Crystallogr. A 47 Pt 2 (1991) 110-119
    • (1991) Acta. Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 29
  • 30
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 31
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 32
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 33747050666 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of central structure domains from Mumps virus F protein
    • Liu Y., Xu Y., Zhu J., Qiu B., Rao Z., Gao G.F., and Tien P. Crystallization and preliminary X-ray diffraction analysis of central structure domains from Mumps virus F protein. Acta Crystallogr. F Biol. Crystallogr. 61 (2005) 855-857
    • (2005) Acta Crystallogr. F Biol. Crystallogr. , vol.61 , pp. 855-857
    • Liu, Y.1    Xu, Y.2    Zhu, J.3    Qiu, B.4    Rao, Z.5    Gao, G.F.6    Tien, P.7
  • 34
    • 0034687711 scopus 로고    scopus 로고
    • Structural characterization of the human respiratory syncytial virus fusion protein core
    • Zhao X., Singh M., Malashkevich V.N., and Kim P.S. Structural characterization of the human respiratory syncytial virus fusion protein core. Proc. Natl. Acad. Sci. USA 97 (2000) 14172-14177
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14172-14177
    • Zhao, X.1    Singh, M.2    Malashkevich, V.N.3    Kim, P.S.4
  • 35
    • 0033618320 scopus 로고    scopus 로고
    • LearnCoil-VMF: computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins
    • Singh M., Berger B., and Kim P.S. LearnCoil-VMF: computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins. J. Mol. Biol. 290 (1999) 1031-1041
    • (1999) J. Mol. Biol. , vol.290 , pp. 1031-1041
    • Singh, M.1    Berger, B.2    Kim, P.S.3


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