메뉴 건너뛰기




Volumn 131, Issue 1, 2007, Pages 70-79

Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice

Author keywords

HUMDISEASE; PROTEINS

Indexed keywords

CAPSID PROTEIN; DIMER; FULLERENE; MUTANT PROTEIN;

EID: 34848866243     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2007.08.018     Document Type: Article
Times cited : (282)

References (53)
  • 2
    • 0020018227 scopus 로고
    • Three-dimensional structure determination by electron microscopy of two-dimensional crystals
    • Amos L.A., Henderson R., and Unwin P.N. Three-dimensional structure determination by electron microscopy of two-dimensional crystals. Prog. Biophys. Mol. Biol. 39 (1982) 183-231
    • (1982) Prog. Biophys. Mol. Biol. , vol.39 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.3
  • 3
    • 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., Sibaï G., Mallet F., and 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    Sibaï, G.4    Mallet, F.5    Cusack, S.6
  • 4
    • 0034954578 scopus 로고    scopus 로고
    • Second-site suppressors of Rous sarcoma virus CA mutations: evidence for interdomain interactions
    • Bowzard J.B., Wills J.W., and Craven R.C. Second-site suppressors of Rous sarcoma virus CA mutations: evidence for interdomain interactions. J. Virol. 75 (2001) 6850-6856
    • (2001) J. Virol. , vol.75 , pp. 6850-6856
    • Bowzard, J.B.1    Wills, J.W.2    Craven, R.C.3
  • 5
    • 84881194271 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals conserved and divergent features of Gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus
    • Briggs J.A.G., Johnson M.C., Simon M.N., Fuller S.D., and Vogt V.M. Cryo-electron microscopy reveals conserved and divergent features of Gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus. J. Mol. Biol. 355 (2006) 157-168
    • (2006) J. Mol. Biol. , vol.355 , pp. 157-168
    • Briggs, J.A.G.1    Johnson, M.C.2    Simon, M.N.3    Fuller, S.D.4    Vogt, V.M.5
  • 7
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • Briggs J.A.G., Wilk T., Welker R., Krausslich H.G., and Fuller S.D. Structural organization of authentic, mature HIV-1 virions and cores. EMBO J. 22 (2003) 1707-1715
    • (2003) EMBO J. , vol.22 , pp. 1707-1715
    • Briggs, J.A.G.1    Wilk, T.2    Welker, R.3    Krausslich, H.G.4    Fuller, S.D.5
  • 8
    • 0034681298 scopus 로고    scopus 로고
    • Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses
    • Campos-Olivas R., Newman J.L., and Summers M.F. Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses. J. Mol. Biol. 296 (2000) 633-649
    • (2000) J. Mol. Biol. , vol.296 , pp. 633-649
    • Campos-Olivas, R.1    Newman, J.L.2    Summers, M.F.3
  • 9
    • 0036297629 scopus 로고    scopus 로고
    • Multi-resolution contour-based fitting of macromolecular structures
    • Chacón P., and Wriggers W. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317 (2002) 375-384
    • (2002) J. Mol. Biol. , vol.317 , pp. 375-384
    • Chacón, P.1    Wriggers, W.2
  • 10
    • 6944256728 scopus 로고    scopus 로고
    • A graphical representation of image quality for three-dimensional structure analysis of two-dimensional crystals
    • Cheng A., and Yeager M. A graphical representation of image quality for three-dimensional structure analysis of two-dimensional crystals. Acta Crystallogr. A 60 (2004) 351-354
    • (2004) Acta Crystallogr. A , vol.60 , pp. 351-354
    • Cheng, A.1    Yeager, M.2
  • 11
    • 0035793720 scopus 로고    scopus 로고
    • Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein
    • Cornilescu C.C., Bouamr F., Yao X., Carter C., and Tjandra N. Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein. J. Mol. Biol. 306 (2000) 783-797
    • (2000) J. Mol. Biol. , vol.306 , pp. 783-797
    • Cornilescu, C.C.1    Bouamr, F.2    Yao, X.3    Carter, C.4    Tjandra, N.5
  • 13
    • 0026762403 scopus 로고
    • Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
    • Ehrlich L.S., Agresta B.E., and 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
  • 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., and 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
    • 0035659634 scopus 로고    scopus 로고
    • The HIV-1 assembly machine
    • Göttlinger H.G. The HIV-1 assembly machine. AIDS 15 Suppl 5 (2001) S13-S20
    • (2001) AIDS , vol.15 , Issue.SUPPL. 5
    • Göttlinger, H.G.1
  • 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., and 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
  • 22
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., and Downing K.H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213 (1990) 899-929
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 23
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacerium halobium: Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution
    • Henderson R., Baldwin J.M., Downing K.H., Lepault J., and Zemlin F. Structure of purple membrane from Halobacerium halobium: Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 19 (1986) 147-178
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 25
    • 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., and 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
  • 27
    • 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., and 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
  • 29
    • 0032863144 scopus 로고    scopus 로고
    • Association of Nef with the human immunodeficiency virus type 1 core
    • Kotov A., Zhou J., Flicker P., and Aiken C. Association of Nef with the human immunodeficiency virus type 1 core. J. Virol. 73 (1999) 8824-8830
    • (1999) J. Virol. , vol.73 , pp. 8824-8830
    • Kotov, A.1    Zhou, J.2    Flicker, P.3    Aiken, C.4
  • 31
  • 33
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li S., Hill C.P., Sundquist W.I., and Finch J.T. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 407 (2000) 409-413
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 35
    • 0036307640 scopus 로고    scopus 로고
    • Analysis of Rous sarcoma virus capsid protein variants assembled on lipid monolayers
    • Mayo K., Vana M.L., McDermott J., Huseby D., Leis J., and Barklis E. Analysis of Rous sarcoma virus capsid protein variants assembled on lipid monolayers. J. Mol. Biol. 316 (2002) 667-678
    • (2002) J. Mol. Biol. , vol.316 , pp. 667-678
    • Mayo, K.1    Vana, M.L.2    McDermott, J.3    Huseby, D.4    Leis, J.5    Barklis, E.6
  • 37
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retroviral capsid hexameric amino-terminal domain
    • Mortuza G.B., Haire L.F., Stevens A., Smerdon S.J., Stoye J.P., and Taylor I.A. High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 431 (2004) 481-485
    • (2004) Nature , vol.431 , pp. 481-485
    • Mortuza, G.B.1    Haire, L.F.2    Stevens, A.3    Smerdon, S.J.4    Stoye, J.P.5    Taylor, I.A.6
  • 38
    • 0034849767 scopus 로고    scopus 로고
    • Analysis of Mason-Pfizer monkey virus Gag particles by scanning transmission electron microscopy
    • Parker S.D., Wall J.S., and Hunter E. Analysis of Mason-Pfizer monkey virus Gag particles by scanning transmission electron microscopy. J. Virol. 75 (2001) 9543-9548
    • (2001) J. Virol. , vol.75 , pp. 9543-9548
    • Parker, S.D.1    Wall, J.S.2    Hunter, E.3
  • 39
    • 0026682511 scopus 로고
    • Characterization of HIV-1 p24 self-association using analytical affinity chromatography
    • Rosé S., Hensley P., O'Shannessy D.J., Culp J., Debouck C., and Chaiken I. Characterization of HIV-1 p24 self-association using analytical affinity chromatography. Proteins 13 (1992) 112-119
    • (1992) Proteins , vol.13 , pp. 112-119
    • Rosé, S.1    Hensley, P.2    O'Shannessy, D.J.3    Culp, J.4    Debouck, C.5    Chaiken, I.6
  • 43
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang C., Ndassa Y., and Summers M.F. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat. Struct. Biol. 9 (2002) 537-543
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 44
    • 33644995225 scopus 로고    scopus 로고
    • The role of subunit hinges and molecular "switches" in the control of viral capsid polymorphism
    • Tang J., Johnson J.M., Dryden K.A., Young M.J., Zlotnick A., and Johnson J.E. The role of subunit hinges and molecular "switches" in the control of viral capsid polymorphism. J. Struct. Biol. 154 (2006) 59-67
    • (2006) J. Struct. Biol. , vol.154 , pp. 59-67
    • Tang, J.1    Johnson, J.M.2    Dryden, K.A.3    Young, M.J.4    Zlotnick, A.5    Johnson, J.E.6
  • 46
    • 0028059991 scopus 로고
    • Analysis of electron microscope images and electron diffraction patterns of thin crystals of phi29 connectors in ice
    • Valpuesta J.M., Carrascosa J.L., and Henderson R. Analysis of electron microscope images and electron diffraction patterns of thin crystals of phi29 connectors in ice. J. Mol. Biol. 240 (1994) 281-287
    • (1994) J. Mol. Biol. , vol.240 , pp. 281-287
    • Valpuesta, J.M.1    Carrascosa, J.L.2    Henderson, R.3
  • 47
    • 0003151659 scopus 로고    scopus 로고
    • Retroviral Virions and Genomes
    • Coffin J.M., Hughes S.H., and Varmus H.E. (Eds), Cold Spring Harbor Press, New York
    • Vogt V. Retroviral Virions and Genomes. In: Coffin J.M., Hughes S.H., and Varmus H.E. (Eds). Retroviruses (1997), Cold Spring Harbor Press, New York 27-70
    • (1997) Retroviruses , pp. 27-70
    • Vogt, V.1
  • 49
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler U.K., Stray K.M., Garrus J.E., and Sundquist W.I. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77 (2003) 5439-5450
    • (2003) J. Virol. , vol.77 , pp. 5439-5450
    • von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 50
    • 0033958427 scopus 로고    scopus 로고
    • Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1
    • Welker R., Hohenberg H., Tessmer U., Huckhagel C., and Kräusslich H.-G. Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1. J. Virol. 74 (2000) 1168-1177
    • (2000) J. Virol. , vol.74 , pp. 1168-1177
    • Welker, R.1    Hohenberg, H.2    Tessmer, U.3    Huckhagel, C.4    Kräusslich, H.-G.5
  • 52
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., and McCammon J.A. Situs: A package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125 (1999) 185-195
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 53
    • 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., and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.