메뉴 건너뛰기




Volumn 286, Issue 1, 1999, Pages 83-93

Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26

Author keywords

Capsid model; Crystal structure; EIAV; HIV; Lentivirus

Indexed keywords

CAPSID PROTEIN; CORE PROTEIN; DIMER; TETRAMER;

EID: 0033548068     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2443     Document Type: Article
Times cited : (104)

References (43)
  • 1
    • 0023645282 scopus 로고
    • Structure of the ColE1 rop protein at 1.7 Å resolution
    • Banner D. W., Kokkinidis M., Tsernoglou D. Structure of the ColE1 rop protein at 1.7 Å resolution. J. Mol. Biol. 196:1987;657-675.
    • (1987) J. Mol. Biol. , vol.196 , pp. 657-675
    • Banner, D.W.1    Kokkinidis, M.2    Tsernoglou, D.3
  • 2
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G. J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 3
    • 0343907286 scopus 로고    scopus 로고
    • Cloning, expression, purification, and characterization of the major core protein (p26) from equine infectious anemia virus
    • Birkett A. J., Yelamos B., Rodriguez-Crespo I., Gavilanes F., Peterson D. L. Cloning, expression, purification, and characterization of the major core protein (p26) from equine infectious anemia virus. Biochim. Biophys. Acta. 1339:1997;62-72.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 62-72
    • Birkett, A.J.1    Yelamos, B.2    Rodriguez-Crespo, I.3    Gavilanes, F.4    Peterson, D.L.5
  • 4
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Bottcher B., Wynne S. A., Crowther R. A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature. 386:1997;88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 5
    • 0029887104 scopus 로고    scopus 로고
    • Cyclophilin A is required for the replication of group M human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus SIV(CPZ)GAB but not group O HIV-1 or other primate immunodeficiency viruses
    • Braaten D., Franke E. K., Luban J. Cyclophilin A is required for the replication of group M human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus SIV(CPZ)GAB but not group O HIV-1 or other primate immunodeficiency viruses. J. Virol. 70:1996;4220-4227.
    • (1996) J. Virol. , vol.70 , pp. 4220-4227
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 7
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar D. L., Klug A. Physical principles in the construction of regular viruses. Cold Spring Harbor Symp. Quant. Biol. 27:1962;1-24.
    • (1962) Cold Spring Harbor Symp. Quant. Biol. , vol.27 , pp. 1-24
    • Caspar, D.L.1    Klug, A.2
  • 8
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C., Lesk A. M. The relation between the divergence of sequence and structure in proteins. EMBO J. 5:1986;823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 9
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway J. F., Cheng N., Zlotnick A., Wingfield P. T., Stahl S. J., Steven A. C. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature. 386:1997;91-94.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 10
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type 1
    • Dorfman T., Bukovsky A., Ohagen A., Hoglund S., Gottlinger H. G. Functional domains of the capsid protein of human immunodeficiency virus type 1. J. Virol. 68:1994;8180-8187.
    • (1994) J. Virol. , vol.68 , pp. 8180-8187
    • Dorfman, T.1    Bukovsky, A.2    Ohagen, A.3    Hoglund, S.4    Gottlinger, H.G.5
  • 11
    • 0025344491 scopus 로고
    • Intracellular proteins of feline immunodeficiency virus and their antigenic relationship with equine infectious anaemia virus proteins
    • Egberink H. F., Ederveen J., Montelaro R. C., Pedersen N. C., Horzinek M. C., Koolen M. J. Intracellular proteins of feline immunodeficiency virus and their antigenic relationship with equine infectious anaemia virus proteins. J. Gen. Virol. 71:1990;739-743.
    • (1990) J. Gen. Virol. , vol.71 , pp. 739-743
    • Egberink, H.F.1    Ederveen, J.2    Montelaro, R.C.3    Pedersen, N.C.4    Horzinek, M.C.5    Koolen, M.J.6
  • 12
    • 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
  • 13
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans S. V. SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138, 127-128.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 14
    • 0029126612 scopus 로고
    • Cyclophilin binding to the human immunodeficiency virus type 1 Gag polyprotein is mimicked by an anti-cyclosporine antibody
    • Franke E. K., Chen B. X., Tatsis I., Diamanduros A., Erlanger B. F., Luban J. Cyclophilin binding to the human immunodeficiency virus type 1 Gag polyprotein is mimicked by an anti-cyclosporine antibody. J. Virol. 69:1995;5821-5823.
    • (1995) J. Virol. , vol.69 , pp. 5821-5823
    • Franke, E.K.1    Chen, B.X.2    Tatsis, I.3    Diamanduros, A.4    Erlanger, B.F.5    Luban, J.6
  • 15
  • 17
    • 0025904765 scopus 로고
    • Assembly and morphology of HIV: Potential effect of structure on viral function
    • Gelderblom H. R. Assembly and morphology of HIV: potential effect of structure on viral function. Aids. 5:1991;617-637.
    • (1991) Aids , vol.5 , pp. 617-637
    • Gelderblom, H.R.1
  • 18
    • 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
  • 19
    • 0023015376 scopus 로고
    • LAV/HTLV-III gag gene product p24 shares antigenic determinants with equine infectious anemia virus but not with visna virus or caprine arthritis encephalitis virus
    • Goudsmit J., Houwers D. J., Smit L., Nauta I. M. LAV/HTLV-III gag gene product p24 shares antigenic determinants with equine infectious anemia virus but not with visna virus or caprine arthritis encephalitis virus. Intervirology. 26:1986;169-173.
    • (1986) Intervirology , vol.26 , pp. 169-173
    • Goudsmit, J.1    Houwers, D.J.2    Smit, L.3    Nauta, I.M.4
  • 20
    • 0030682425 scopus 로고    scopus 로고
    • In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus
    • Gross I., Hohenberg H., Krausslich 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    Krausslich, H.G.3
  • 21
    • 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., Krausslich 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    Krausslich, H.G.4
  • 22
    • 0023152815 scopus 로고
    • Chemical and immunological characterizations of equine infectious anemia virus gag-encoded proteins
    • Henderson L. E., Sowder R. C., Smythers G. W., Oroszlan S. Chemical and immunological characterizations of equine infectious anemia virus gag-encoded proteins. J. Virol. 61:1987;1116-1124.
    • (1987) J. Virol. , vol.61 , pp. 1116-1124
    • Henderson, L.E.1    Sowder, R.C.2    Smythers, G.W.3    Oroszlan, S.4
  • 25
    • 0024722728 scopus 로고
    • Topological distribution of four-alpha-helix bundles
    • Presnell S. R., Cohen F. E. Topological distribution of four-alpha-helix bundles. Proc. Natl Acad. Sci. USA. 86:1989;6592-6596.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6592-6596
    • Presnell, S.R.1    Cohen, F.E.2
  • 27
    • 0031045818 scopus 로고    scopus 로고
    • Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement
    • C. W. Carter, & R. M. Sweet. San Diego: Academic Press
    • Ramakrishnan V., Biou V. Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement. Carter C. W., Sweet R. M. Methods in Enzymology. 1997;538-557 Academic Press, San Diego.
    • (1997) Methods in Enzymology , pp. 538-557
    • Ramakrishnan, V.1    Biou, V.2
  • 28
    • 0028873674 scopus 로고
    • Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: Effects on virion particle assembly, release, and infectivity
    • Reicin A. S., Paik S., Berkowitz R. D., Luban J., Lowy I., Goff S. P. Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: effects on virion particle assembly, release, and infectivity. J. Virol. 69:1995;642-650.
    • (1995) J. Virol. , vol.69 , pp. 642-650
    • Reicin, A.S.1    Paik, S.2    Berkowitz, R.D.3    Luban, J.4    Lowy, I.5    Goff, S.P.6
  • 29
    • 0029961364 scopus 로고    scopus 로고
    • The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle
    • Reicin A. S., Ohagen A., Yin L., Hoglund S., Goff S. P. The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle. J. Virol. 70:1996;8645-8652.
    • (1996) J. Virol. , vol.70 , pp. 8645-8652
    • Reicin, A.S.1    Ohagen, A.2    Yin, L.3    Hoglund, S.4    Goff, S.P.5
  • 30
    • 0024340454 scopus 로고
    • The preparation and biochemical characterization of intact capsids of equine infectious anemia virus
    • Roberts M. M., Oroszlan S. The preparation and biochemical characterization of intact capsids of equine infectious anemia virus. Biochem. Biophys. Res. Commun. 160:1989;486-494.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 486-494
    • Roberts, M.M.1    Oroszlan, S.2
  • 32
    • 0008238291 scopus 로고
    • Antiviral agents targeted to interact with viral capsid proteins and a possible application to human immunodeficiency virus
    • Rossmann M. G. Antiviral agents targeted to interact with viral capsid proteins and a possible application to human immunodeficiency virus. Proc. Natl Acad. Sci. USA. 85:1988;4625-4627.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4625-4627
    • Rossmann, M.G.1
  • 34
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman J. L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 253:1991;872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 36
    • 0030666230 scopus 로고    scopus 로고
    • Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein
    • Vajdos F. F., Yoo S., Houseweart M., Sundquist W. I., Hill C. P. Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein. Protein Sci. 6:1997;2297-2307.
    • (1997) Protein Sci. , vol.6 , pp. 2297-2307
    • Vajdos, F.F.1    Yoo, S.2    Houseweart, M.3    Sundquist, W.I.4    Hill, C.P.5
  • 38
    • 0027160015 scopus 로고
    • Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants
    • Wang C. T., Barklis E. Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants. J. Virol. 67:1993;4264-4273.
    • (1993) J. Virol. , vol.67 , pp. 4264-4273
    • Wang, C.T.1    Barklis, E.2
  • 39
    • 0019316535 scopus 로고
    • Structural and functional diversity in 4-alpha-helical proteins
    • Weber P. C., Salemme F. R. Structural and functional diversity in 4-alpha-helical proteins. Nature. 287:1980;82-84.
    • (1980) Nature , vol.287 , pp. 82-84
    • Weber, P.C.1    Salemme, F.R.2
  • 40
    • 0031925586 scopus 로고    scopus 로고
    • Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites
    • Wiegers K., Rutter G., Kottler H., Tessmer U., Hohenberg H., Krausslich H. G. Sequential steps in human immunodeficiency virus particle maturation 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    Krausslich, H.G.6
  • 41
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral gag
    • Wills J. W., Craven R. C. Form, function, and use of retroviral gag. Aids. 5:1991;639-654.
    • (1991) Aids , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 42
    • 0032560502 scopus 로고    scopus 로고
    • Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: Implications for retroviral assembly mechanisms
    • Yeager M., Wilson-Kubalek E. M., Weiner S. G., Brown P. O., Rein A. Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms. Proc. Natl Acad. Sci. USA. 95:1998;7299-7304.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7299-7304
    • Yeager, M.1    Wilson-Kubalek, E.M.2    Weiner, S.G.3    Brown, P.O.4    Rein, A.5
  • 43
    • 0030930426 scopus 로고    scopus 로고
    • Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: Implications for morphogenesis and organization of encapsidated RNA
    • Zlotnick A., Cheng N., Stahl S. J., Conway J. F., Steven A. C., Wingfield P. T. Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: implications for morphogenesis and organization of encapsidated RNA. Proc. Natl Acad. Sci. USA. 94:1997;9556-9561.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9556-9561
    • Zlotnick, A.1    Cheng, N.2    Stahl, S.J.3    Conway, J.F.4    Steven, A.C.5    Wingfield, P.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.