메뉴 건너뛰기




Volumn 8, Issue 6, 2000, Pages 617-628

Structure and self-association of the Rous sarcoma virus capsid protein

Author keywords

Election microscopy; NMR spectroscopy; Retrovirus; Self assembly; X ray crystallography

Indexed keywords

CAPSID PROTEIN;

EID: 0034659842     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00148-9     Document Type: Article
Times cited : (103)

References (53)
  • 2
    • 0033117918 scopus 로고    scopus 로고
    • Towards the structure of the human immunodeficiency virus: Divide and conquer?
    • Wilk T., Fuller S.D. Towards the structure of the human immunodeficiency virus: divide and conquer? Curr. Opin. Struct. Biol. 9:1999;231-243.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 231-243
    • Wilk, T.1    Fuller, S.D.2
  • 3
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble T.R., Hill C.P.et al. Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell. 87:1996;1285-1294.
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1    Hill, C.P.2
  • 4
    • 0029794123 scopus 로고    scopus 로고
    • Structure of the amino-terminal core domain of the HIV-1 capsid protein
    • Gitti R.K., Lee B.M., Walker J., Summers M.F., Yoo S., Sundquist W.I. Structure of the amino-terminal core domain of the HIV-1 capsid protein. Science. 273:1996;231-235.
    • (1996) Science , vol.273 , pp. 231-235
    • Gitti, R.K.1    Lee, B.M.2    Walker, J.3    Summers, M.F.4    Yoo, S.5    Sundquist, W.I.6
  • 5
    • 16044367113 scopus 로고    scopus 로고
    • Crystal structure of dimeric HIV-1 capsid protein
    • Momany C., Rossmann M.G.et al. Crystal structure of dimeric HIV-1 capsid protein. Nat. Struct. Biol. 3:1996;763-770.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 763-770
    • Momany, C.1    Rossmann, M.G.2
  • 6
    • 0030693391 scopus 로고    scopus 로고
    • Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
    • Gamble T.R., Hill C.P.et al. Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein. Science. 278:1997;849-853.
    • (1997) Science , vol.278 , pp. 849-853
    • Gamble, T.R.1    Hill, C.P.2
  • 7
    • 0033106192 scopus 로고    scopus 로고
    • Head-to-tail dimers and interdomain flexibility revealed by the crystal structure of HIV-1 capsid protein (p24) complexed with a monoclonal antibody Fab
    • Berthet-Colominas C., Monaco S., Novelli A., Siba G., Mallet F., Cusack S. Head-to-tail dimers and interdomain flexibility revealed by the crystal structure of HIV-1 capsid protein (p24) complexed with a monoclonal antibody Fab. EMBO J. 18:1999;1124-1136.
    • (1999) EMBO J. , vol.18 , pp. 1124-1136
    • Berthet-Colominas, C.1    Monaco, S.2    Novelli, A.3    Siba, G.4    Mallet, F.5    Cusack, S.6
  • 8
  • 9
    • 0033548068 scopus 로고    scopus 로고
    • Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26
    • Jin Z., Jin L., Peterson D.L., Lawson C.L. Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26. J. Mol. Biol. 286:1999;83-93.
    • (1999) J. Mol. Biol. , vol.286 , pp. 83-93
    • Jin, Z.1    Jin, L.2    Peterson, D.L.3    Lawson, C.L.4
  • 10
    • 0032781006 scopus 로고    scopus 로고
    • Solution structure of the capsid protein from the human T-cell leukemia virus type-I
    • Khorasanizadeh S., Campos-Olivas R., Summers M.F. Solution structure of the capsid protein from the human T-cell leukemia virus type-I. J. Mol. Biol. 291:1999;491-505.
    • (1999) J. Mol. Biol. , vol.291 , pp. 491-505
    • Khorasanizadeh, S.1    Campos-Olivas, R.2    Summers, M.F.3
  • 11
    • 0028342554 scopus 로고
    • Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis
    • Mammano F., Öhagen Å., Höglund S., Göttlinger H.G. Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis. J. Virol. 68:1994;4927-4936.
    • (1994) J. Virol. , vol.68 , pp. 4927-4936
    • Mammano, F.1    Öhagen, Å.2    Höglund, S.3    Göttlinger, H.G.4
  • 12
    • 0029015825 scopus 로고
    • Genetic analysis of the major homology region of Rous sarcoma virus Gag protein
    • Craven R.C., Leure-duPree A.E., Weldon R.A.J., Wills J.W. Genetic analysis of the major homology region of Rous sarcoma virus Gag protein. J. Virol. 69:1995;4213-4227.
    • (1995) J. Virol. , vol.69 , pp. 4213-4227
    • Craven, R.C.1    Leure-Dupree, A.E.2    Weldon, R.A.J.3    Wills, J.W.4
  • 13
    • 0031964529 scopus 로고    scopus 로고
    • Genetic determinants of Rous sarcoma virus particle size
    • Krishna N.K., Campbell S., Vogt V.M., Wills J.W. Genetic determinants of Rous sarcoma virus particle size. J. Virol. 72:1998;564-577.
    • (1998) J. Virol. , vol.72 , pp. 564-577
    • Krishna, N.K.1    Campbell, S.2    Vogt, V.M.3    Wills, J.W.4
  • 14
    • 0027236919 scopus 로고
    • Necessity of the spacer peptide between CA and NC in the Rous sarcoma virus Gag protein
    • Craven R.C., Leure-duPree A.E., Erdie C.R., Wilson C.B., Wills J.W. Necessity of the spacer peptide between CA and NC in the Rous sarcoma virus Gag protein. J. Virol. 67:1993;6246-6252.
    • (1993) J. Virol. , vol.67 , pp. 6246-6252
    • Craven, R.C.1    Leure-Dupree, A.E.2    Erdie, C.R.3    Wilson, C.B.4    Wills, J.W.5
  • 15
    • 0029166751 scopus 로고
    • Differential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses
    • Pepinsky R.B., Papayannopoulos I.A., Chow E.P., Krishna N.K., Craven R.C., Vogt V.M. Differential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses. J. Virol. 69:1995;6430-6438.
    • (1995) J. Virol. , vol.69 , pp. 6430-6438
    • Pepinsky, R.B.1    Papayannopoulos, I.A.2    Chow, E.P.3    Krishna, N.K.4    Craven, R.C.5    Vogt, V.M.6
  • 16
    • 2642607039 scopus 로고    scopus 로고
    • A putative α-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly
    • Accola M.A., Höglund S., Göttlinger H.G. A putative α-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly. J. Virol. 72:1998;2072-2078.
    • (1998) J. Virol. , vol.72 , pp. 2072-2078
    • Accola, M.A.1    Höglund, S.2    Göttlinger, H.G.3
  • 17
    • 0031925586 scopus 로고    scopus 로고
    • Sequential steps in human immunodeficiency virus particle release revealed by alterations of individual Gag polyprotein cleavage sites
    • Wiegers K., Rutter G., Kottler H., Tessmer U., Hohenberg H., Kräusslich H.G. Sequential steps in human immunodeficiency virus particle release revealed by alterations of individual Gag polyprotein cleavage sites. J. Virol. 72:1998;2846-2854.
    • (1998) J. Virol. , vol.72 , pp. 2846-2854
    • Wiegers, K.1    Rutter, G.2    Kottler, H.3    Tessmer, U.4    Hohenberg, H.5    Kräusslich, H.G.6
  • 18
    • 0031564071 scopus 로고    scopus 로고
    • Crystals of Rous sarcoma virus capsid protein show a helical arrangement of protein subunits
    • Kovari L.C., Rossmann M.G.et al. Crystals of Rous sarcoma virus capsid protein show a helical arrangement of protein subunits. Virology. 238:1997;79-84.
    • (1997) Virology , vol.238 , pp. 79-84
    • Kovari, L.C.1    Rossmann, M.G.2
  • 19
    • 0033543151 scopus 로고    scopus 로고
    • Backbone dynamics of the N-terminal domain of the HIV-1 capsid protein and comparison with the G94D mutant conferring cyclosporin resistance/dependence
    • Campos-Olivas R., Summers M.F. Backbone dynamics of the N-terminal domain of the HIV-1 capsid protein and comparison with the G94D mutant conferring cyclosporin resistance/dependence. Biochemistry. 38:1999;10262-10271.
    • (1999) Biochemistry , vol.38 , pp. 10262-10271
    • Campos-Olivas, R.1    Summers, M.F.2
  • 20
    • 0031954466 scopus 로고    scopus 로고
    • N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles
    • Gross I., Hohenberg H., Huckhagel C., Kräusslich H.G. N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J. Virol. 72:1998;4798-4810.
    • (1998) J. Virol. , vol.72 , pp. 4798-4810
    • Gross, I.1    Hohenberg, H.2    Huckhagel, C.3    Kräusslich, H.G.4
  • 21
    • 0030947591 scopus 로고    scopus 로고
    • In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: Identification of the p10 domain as a morphological determinant in the formation of spherical particles
    • Campbell S., Vogt V.M. In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles. J. Virol. 71:1997;4425-4435.
    • (1997) J. Virol. , vol.71 , pp. 4425-4435
    • Campbell, S.1    Vogt, V.M.2
  • 22
    • 0034602834 scopus 로고    scopus 로고
    • A conformational switch controlling HIV-1 morphogenesis
    • Gross I., Kräusslich H.G.et al. A conformational switch controlling HIV-1 morphogenesis. EMBO J. 19:2000;103-113.
    • (2000) EMBO J. , vol.19 , pp. 103-113
    • Gross, I.1    Kräusslich, H.G.2
  • 23
    • 0033529861 scopus 로고    scopus 로고
    • Intrinsic β-sheet propensities result from van der Waals interactions between sidechains and the local backbone
    • Street A.G., Mayo S.L. Intrinsic β-sheet propensities result from van der Waals interactions between sidechains and the local backbone. Proc. Natl Acad. Sci. USA. 96:1999;9074-9076.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9074-9076
    • Street, A.G.1    Mayo, S.L.2
  • 25
    • 0021112599 scopus 로고
    • Localization of lipid-protein and protein-protein interactions within the murine retrovirus gag precursor by a novel peptide-mapping technique
    • Pepinsky R.B. Localization of lipid-protein and protein-protein interactions within the murine retrovirus gag precursor by a novel peptide-mapping technique. J. Biol. Chem. 258:1983;11229-11235.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11229-11235
    • Pepinsky, R.B.1
  • 26
    • 0026762403 scopus 로고
    • Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
    • Ehrlich L.S., Agresta B.E., Carter C.A. Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro. J. Virol. 66:1992;4874-4883.
    • (1992) J. Virol. , vol.66 , pp. 4874-4883
    • Ehrlich, L.S.1    Agresta, B.E.2    Carter, C.A.3
  • 27
    • 0030682425 scopus 로고    scopus 로고
    • In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus
    • Gross I., Hohenberg H., Kräusslich H.G. In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus. Eur. J. Biochem. 249:1997;592-600.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 592-600
    • Gross, I.1    Hohenberg, H.2    Kräusslich, H.G.3
  • 28
    • 0041925439 scopus 로고    scopus 로고
    • In vitro assembly properties of wild-type and cyclophilin-binding defective human immunodeficiency virus capsid proteins in the presence and absence of cyclophilin A
    • Grättinger M., Hohenberg H., Thomas D., Wilk T., Müller B., Kräusslich H.G. In vitro assembly properties of wild-type and cyclophilin-binding defective human immunodeficiency virus capsid proteins in the presence and absence of cyclophilin A. Virology. 257:1999;247-260.
    • (1999) Virology , vol.257 , pp. 247-260
    • Grättinger, M.1    Hohenberg, H.2    Thomas, D.3    Wilk, T.4    Müller, B.5    Kräusslich, H.G.6
  • 30
    • 0020594561 scopus 로고
    • Nucleotide sequence of Rous sarcoma virus
    • Schwartz D.E., Tizard R., Gilbert W. Nucleotide sequence of Rous sarcoma virus. Cell. 32:1983;853-869.
    • (1983) Cell , vol.32 , pp. 853-869
    • Schwartz, D.E.1    Tizard, R.2    Gilbert, W.3
  • 31
    • 0000122663 scopus 로고
    • Search designs for protein crystallization based on orthogonal arrays
    • Kingston R.L., Baker H.M., Baker E.N. Search designs for protein crystallization based on orthogonal arrays. Acta Crystallogr. D. 50:1994;429-440.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 429-440
    • Kingston, R.L.1    Baker, H.M.2    Baker, E.N.3
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 0343948653 scopus 로고
    • Refinement of single isomorphous replacement heavy-atom parameters in Patterson vs reciprocal space
    • W. Wolf, P.R. Evans, & A.G.W. Leslie. Daresbury: Science and Engineering Research Council
    • Tickle I.J. Refinement of single isomorphous replacement heavy-atom parameters in Patterson vs reciprocal space. Wolf W., Evans P.R., Leslie A.G.W. Isomorphous Replacement and Anomalous Scattering. Proceedings of the CCP4 Study Weekend, 25-26 January 1991. 1991;87-95 Science and Engineering Research Council, Daresbury.
    • (1991) Isomorphous Replacement and Anomalous Scattering. Proceedings of the CCP4 Study Weekend, 25-26 January 1991 , pp. 87-95
    • Tickle, I.J.1
  • 34
    • 84943920736 scopus 로고
    • Phase annealing in SHELX-90: Direct methods for larger structures
    • Sheldrick G.M. Phase annealing in SHELX-90: direct methods for larger structures. Acta Crystallogr. A. 46:1990;467-473.
    • (1990) Acta Crystallogr. a , vol.46 , pp. 467-473
    • Sheldrick, G.M.1
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 37
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:1999;156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 38
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger A.T., Warren G.L.et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D. 54:1998;905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 39
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang J.S., Brünger A.T. Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243:1994;100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brünger, A.T.2
  • 41
    • 0028204451 scopus 로고
    • Solution structure and dynamics of Ras p21·GDP determined by heteronuclear three- And four-dimensional NMR spectroscopy
    • Kraulis P.J., Domaille P.J., Campbell-Burk S.L., Van Aken T., Laue E.D. Solution structure and dynamics of Ras p21·GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 33:1994;3515-3531.
    • (1994) Biochemistry , vol.33 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 43
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from β-spectrin
    • Nilges M., Macias M.J., O'Donoghue S.I., Oschkinat H. Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin. J. Mol. Biol. 269:1997;408-422.
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    MacIas, M.J.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 44
    • 0028673482 scopus 로고
    • Measurement of homo- And heteronuclear J couplings from quantitative J correlation
    • Bax A., Zhu G.et al. Measurement of homo- and heteronuclear J couplings from quantitative J correlation. Methods Enzymol. 239:1994;79-105.
    • (1994) Methods Enzymol. , vol.239 , pp. 79-105
    • Bax, A.1    Zhu, G.2
  • 46
    • 0028432974 scopus 로고
    • The impact of direct refinement against three-bond HN-CαH coupling constants on protein structure determination by NMR
    • Garret D.S., Clore G.M.et al. The impact of direct refinement against three-bond HN-CαH coupling constants on protein structure determination by NMR. J. Magn. Reson. B. 104:1994;99-103.
    • (1994) J. Magn. Reson. B , vol.104 , pp. 99-103
    • Garret, D.S.1    Clore, G.M.2
  • 47
    • 0029351467 scopus 로고
    • J-coupling restraint potentials for nonstereospecifically assigned methylene protons and ensemble-average calculations
    • Constantine K.L., Friedrichs M.S., Mueller L., Bruccoleri R.E. J-coupling restraint potentials for nonstereospecifically assigned methylene protons and ensemble-average calculations. J. Magn. Reson. B. 108:1995;176-184.
    • (1995) J. Magn. Reson. B , vol.108 , pp. 176-184
    • Constantine, K.L.1    Friedrichs, M.S.2    Mueller, L.3    Bruccoleri, R.E.4
  • 48
    • 0030191673 scopus 로고    scopus 로고
    • A potential involving multiple proton chemical-shift restraints for nonstereospecifically assigned methyl and methylene protons
    • Kuszewski J., Gronenborn A.M., Clore G.M. A potential involving multiple proton chemical-shift restraints for nonstereospecifically assigned methyl and methylene protons. J. Magn. Reson. B. 112:1996;79-81.
    • (1996) J. Magn. Reson. B , vol.112 , pp. 79-81
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 49
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain rotamer preferences
    • Dunbrack R.L.J., Cohen F.E. Bayesian statistical analysis of protein side-chain rotamer preferences. Protein Sci. 6:1997;1661-1681.
    • (1997) Protein Sci. , vol.6 , pp. 1661-1681
    • Dunbrack, R.L.J.1    Cohen, F.E.2
  • 51
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. 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.1
  • 53
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner M.F., Olson A.J., Spehner J.C. Reduced surface: an efficient way to compute molecular surfaces. Biopolymers. 38:1996;305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.