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Volumn 5, Issue 1, 1997, Pages 139-146

Cyclophilin A complexed with a fragment of HIV-1 gag protein: Insights into HIV-1 infectious activity

Author keywords

chaperone; cis trans isomerization; immunophilin; X ray crystallography

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; MIRIDAE;

EID: 0031568329     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00172-X     Document Type: Article
Times cited : (77)

References (51)
  • 1
    • 0021159379 scopus 로고
    • Cyclophilin: A specific cytosolic binding protein for cyclosporin A
    • Handschumacher, R.E., Harding, M.W., Rice, J. & Drugge, R.J. (1984). Cyclophilin: a specific cytosolic binding protein for cyclosporin A. Science 226, 544-547.
    • (1984) Science , vol.226 , pp. 544-547
    • Handschumacher, R.E.1    Harding, M.W.2    Rice, J.3    Drugge, R.J.4
  • 2
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T. & Schmid, F.X. (1989). Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337, 476-478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 3
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi, N., Hayano, T. & Suzuki, M. (1989). Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 337, 473-475.
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 5
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu, J., Farmer, J.D., Jr., Lane, W.S., Friedman, J., Weissman, I. & Schreiber, S.L. (1991). Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66, 807-815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer Jr., J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 6
    • 0025831980 scopus 로고
    • Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: One in the presence and one in the absence of CsA
    • Friedman, J. & Weissman, I. (1991). Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: one in the presence and one in the absence of CsA. Cell 66, 799-806.
    • (1991) Cell , vol.66 , pp. 799-806
    • Friedman, J.1    Weissman, I.2
  • 7
    • 0025260865 scopus 로고
    • The mechanism of protein folding. Implications of in vitro refolding model for de novo protein folding and translocation in the cell
    • Fischer, G. & Schmid, F.X. (1990). The mechanism of protein folding. Implications of in vitro refolding model for de novo protein folding and translocation in the cell. Biochemistry 29, 2205-2212.
    • (1990) Biochemistry , vol.29 , pp. 2205-2212
    • Fischer, G.1    Schmid, F.X.2
  • 9
    • 0023657312 scopus 로고
    • The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen
    • Bächinger, H.P. (1987). The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. J. Biol. Chem. 262, 17144-17148.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17144-17148
    • Bächinger, H.P.1
  • 10
    • 0024339276 scopus 로고
    • Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans isomerase on the folding of the triple helix
    • Davis, J.M., Boswell, B.A. & Bächinger, H.P. (1989). Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans isomerase on the folding of the triple helix. J. Biol. Chem. 264, 8956-8962.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8956-8962
    • Davis, J.M.1    Boswell, B.A.2    Bächinger, H.P.3
  • 11
    • 0026526853 scopus 로고
    • Cis-trans isomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase
    • Fransson, C., et al., & Carlsson, U. (1992). Cis-trans isomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase. FEBS Lett. 296, 90-94.
    • (1992) FEBS Lett. , vol.296 , pp. 90-94
    • Fransson, C.1    Carlsson, U.2
  • 12
    • 0026342150 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
    • Jackson, S.E. & Fersht, A.R. (1991). Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding. Biochemistry 30, 10436-10443.
    • (1991) Biochemistry , vol.30 , pp. 10436-10443
    • Jackson, S.E.1    Fersht, A.R.2
  • 13
    • 0025195733 scopus 로고
    • Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization
    • Kiefhaber, T., Quaas, R., Hahn, U. & Schmid, F.X. (1990). Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization. Biochemistry 29, 3053-3061.
    • (1990) Biochemistry , vol.29 , pp. 3053-3061
    • Kiefhaber, T.1    Quaas, R.2    Hahn, U.3    Schmid, F.X.4
  • 14
    • 0023236959 scopus 로고
    • Catalysis of protein folding by prolyl isomerase
    • Lang, K., Schmid, F.X. & Fischer, G. (1987). Catalysis of protein folding by prolyl isomerase. Nature 329, 268-270.
    • (1987) Nature , vol.329 , pp. 268-270
    • Lang, K.1    Schmid, F.X.2    Fischer, G.3
  • 16
    • 0025968746 scopus 로고
    • Cyclosporin A slows collagen triple-helixformation in vitro: Indirect evidence for a physiologic role of peptidyl-prolyl cis-trans isomerase
    • Steinmann, B., Bruchner, P. & Superti-Furga, A. (1991). Cyclosporin A slows collagen triple-helixformation in vitro: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans isomerase. J. Biol. Chem. 266, 1299-1303.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1299-1303
    • Steinmann, B.1    Bruchner, P.2    Superti-Furga, A.3
  • 17
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker, E.K., Colley, N.J. & Zuker, C.S. (1994). The cyclophilin homolog NinaA functions as chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J. 13, 4886-4895.
    • (1994) EMBO J. , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 18
    • 0028027504 scopus 로고
    • A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23
    • Johnson, J.L. & Toft, D.O. (1994). A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23. J. Biol. Chem. 269, 24989-24993.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24989-24993
    • Johnson, J.L.1    Toft, D.O.2
  • 19
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 gag protein binds to cyclophilins A and B
    • Luban, J., Bossolt, K.L., Franke, E.K., Kalpana, G.V. & Goff, S.P. (1993). Human immunodeficiency virus type 1 gag protein binds to cyclophilins A and B. Cell 73, 1067-1078.
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 20
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke, E.K., Yuan, H.E.H. & Luban, J. (1994). Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372, 359-362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 21
    • 0027971782 scopus 로고
    • Functional association of cyclophilin A with HIV-1 virions
    • Thall, M., et al., & Göttlinger, H.G. (1994). Functional association of cyclophilin A with HIV-1 virions. Nature 372, 363-365.
    • (1994) Nature , vol.372 , pp. 363-365
    • Thall, M.1    Göttlinger, H.G.2
  • 22
    • 0029887104 scopus 로고    scopus 로고
    • Cyclophilin A is required for the replication of group M human immunodeficiency virus type 1 (HIV-1) and simiam immunodeficiency virus SIVcpzGAB but not group O HIV-1 or other primate immunodeficiency viruses
    • Braaten, D., Franke, E.K. & Luban, J. (1996). Cyclophilin A is required for the replication of group M human immunodeficiency virus type 1 (HIV-1) and simiam immunodeficiency virus SIVcpzGAB but not group O HIV-1 or other primate immunodeficiency viruses. J. Virol. 70, 4220-4227.
    • (1996) J. Virol. , vol.70 , pp. 4220-4227
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 23
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral gag proteins
    • Wills, J.W. & Craven, R.C. (1991). Form, function, and use of retroviral gag proteins. AIDS 5, 639-654.
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 24
    • 0025904765 scopus 로고
    • Assembly and morphology of HIV: Potential effect of structure on viral function
    • Gelderblom, H.R. (1991). Assembly and morphology of HIV: potential effect of structure on viral function. AIDS 5, 617-638.
    • (1991) AIDS , vol.5 , pp. 617-638
    • Gelderblom, H.R.1
  • 25
    • 0029126612 scopus 로고
    • Cyclophilin binding to human immunodeficiency virus type 1 gag polyprotein is mimicked by an anti-cyclosporin antibody
    • Franke, E.K., Chen, A., Tatsis, I., Diamanduros, A., Erlanger, B. & Luban, J. (1995). Cyclophilin binding to human immunodeficiency virus type 1 gag polyprotein is mimicked by an anti-cyclosporin antibody. J. Virol. 69, 5821-5823.
    • (1995) J. Virol. , vol.69 , pp. 5821-5823
    • Franke, E.K.1    Chen, A.2    Tatsis, I.3    Diamanduros, A.4    Erlanger, B.5    Luban, J.6
  • 26
    • 0029948529 scopus 로고    scopus 로고
    • Binding of human immunodeficiency virus type 1 gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires gag dimerization
    • Colgan, J., Yuan, H.E.H., Franke, E.K. & Luban, J. (1996). Binding of human immunodeficiency virus type 1 gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires gag dimerization. J. Virol. 70, 4220-4227.
    • (1996) J. Virol. , vol.70 , pp. 4220-4227
    • Colgan, J.1    Yuan, H.E.H.2    Franke, E.K.3    Luban, J.4
  • 27
    • 0029949799 scopus 로고    scopus 로고
    • Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription
    • Braaten, D, Franke, E.K. & Luban, J. (1996). Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription. J. Virol. 70, 3551-3560.
    • (1996) J. Virol. , vol.70 , pp. 3551-3560
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 28
    • 0029794123 scopus 로고    scopus 로고
    • Structure of amino-terminal core domain of the HIV-1 capsid protein
    • Gitti, R.K., Lee, B.M., Walker, J., Summers, M.F., Yoo, S. & Sundquis, W.I. (1996). Structure of amino-terminal core domain of the HIV-1 capsid protein. Science 273, 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    Sundquis, W.I.6
  • 29
    • 16044367113 scopus 로고    scopus 로고
    • Crystal structure of dimeric HIV-1 capsid protein
    • Momany, C., et al., & Rossmann, M.G. (1996). Crystal structure of dimeric HIV-1 capsid protein. Nat. Struct. Biol. 3, 763-770.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 763-770
    • Momany, C.1    Rossmann, M.G.2
  • 30
    • 0026042453 scopus 로고
    • Crystal structure of recombinant human T-cell cyclophilin A at 2.5 Å resolution
    • Ke, H., Zydowsky, L.D., Liu, J. & Walsh, C.T. (1991). Crystal structure of recombinant human T-cell cyclophilin A at 2.5 Å resolution. Proc. Natl. Acad. Sci. USA 88, 9483-9487.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9483-9487
    • Ke, H.1    Zydowsky, L.D.2    Liu, J.3    Walsh, C.T.4
  • 31
    • 0026619463 scopus 로고
    • Similarities and differences between human cyclophilin A and other β-barrel structures: Structural refinement at 1.63 Å resolution
    • Ke, H. (1992). Similarities and differences between human cyclophilin A and other β-barrel structures: structural refinement at 1.63 Å resolution. J. Mol. Biol. 228, 539-550.
    • (1992) J. Mol. Biol. , vol.228 , pp. 539-550
    • Ke, H.1
  • 32
    • 0025858482 scopus 로고
    • Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy
    • Kallen, J., et al., & Walkinshaw, M.D. (1991). Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature 353, 276-279.
    • (1991) Nature , vol.353 , pp. 276-279
    • Kallen, J.1    Walkinshaw, M.D.2
  • 33
    • 0026532431 scopus 로고
    • The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A
    • Kallen, J. & Walkinshaw, M.D. (1992). The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A. FEBS Lett. 300, 286-290.
    • (1992) FEBS Lett. , vol.300 , pp. 286-290
    • Kallen, J.1    Walkinshaw, M.D.2
  • 34
    • 0027483416 scopus 로고
    • Crystal structure of cyclophilin A complexed with substrate Ala-Pro suggests a solvent-assisted mechanism of cis-trans isomerization
    • Ke, H.M., Mayrose, D. & Cao, W. (1993). Crystal structure of cyclophilin A complexed with substrate Ala-Pro suggests a solvent-assisted mechanism of cis-trans isomerization. Proc. Natl. Acad. Sci. USA 90, 3324-3328.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3324-3328
    • Ke, H.M.1    Mayrose, D.2    Cao, W.3
  • 35
    • 0030014678 scopus 로고    scopus 로고
    • Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes
    • Zhao, Y. & Ke, H.M. (1996). Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes. Biochemistry 35, 7362-7368.
    • (1996) Biochemistry , vol.35 , pp. 7362-7368
    • Zhao, Y.1    Ke, H.M.2
  • 36
    • 0029970349 scopus 로고    scopus 로고
    • The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer
    • Konno, M., Ito, M., Hayano, T. & Takahashi, N. (1996). The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer. J. Mol. Biol. 256, 897-908.
    • (1996) J. Mol. Biol. , vol.256 , pp. 897-908
    • Konno, M.1    Ito, M.2    Hayano, T.3    Takahashi, N.4
  • 37
    • 0029982651 scopus 로고    scopus 로고
    • Crystal structure implies that cyclophilin predominantly catalyzes the frans to cis isomerization
    • Zhao, Y. & Ke, H.M. (1996). Crystal structure implies that cyclophilin predominantly catalyzes the frans to cis isomerization. Biochemistry 35, 7356-7361.
    • (1996) Biochemistry , vol.35 , pp. 7356-7361
    • Zhao, Y.1    Ke, H.M.2
  • 39
    • 0028772888 scopus 로고
    • Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethyl-threonine cyclosporin A
    • Ke, H., et al., & Walsh, C.T. (1994). Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethyl-threonine cyclosporin A. Structure 2, 33-44.
    • (1994) Structure , vol.2 , pp. 33-44
    • Ke, H.1    Walsh, C.T.2
  • 40
    • 0027397418 scopus 로고
    • Solution structure of the cyclosporin A/cyclophilin complex by NMR
    • Thèriault, Y., et al., & Fesik, S.W. (1993). Solution structure of the cyclosporin A/cyclophilin complex by NMR. Nature 361, 88-91.
    • (1993) Nature , vol.361 , pp. 88-91
    • Thèriault, Y.1    Fesik, S.W.2
  • 42
    • 0027772159 scopus 로고
    • X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 Å resolution
    • Mikol, V., Kallen, J., Pflügl, G. & Walkinshaw, M.D. (1993). X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 Å resolution. J. Mol. Biol. 234, 1119-1130.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1119-1130
    • Mikol, V.1    Kallen, J.2    Pflügl, G.3    Walkinshaw, M.D.4
  • 43
    • 0028265670 scopus 로고
    • Solution conformation of a cyclophilin-bound proline isomerase substrate
    • Kakalis, L.T. & Armitage, I.M. (1994). Solution conformation of a cyclophilin-bound proline isomerase substrate. Biochemistry 33, 1495-1501.
    • (1994) Biochemistry , vol.33 , pp. 1495-1501
    • Kakalis, L.T.1    Armitage, I.M.2
  • 44
    • 0030574036 scopus 로고    scopus 로고
    • Extended binding sites of cyclophilin as revealed by the interaction with HIV-1 gag polyprotein derived oligopeptide
    • Schutkowski, M., et al., & Fischer, G. (1996). Extended binding sites of cyclophilin as revealed by the interaction with HIV-1 gag polyprotein derived oligopeptide. FEBS Lett. 394, 289-294.
    • (1996) FEBS Lett. , vol.394 , pp. 289-294
    • Schutkowski, M.1    Fischer, G.2
  • 45
    • 0025216877 scopus 로고
    • Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis
    • Liu, J., Albers, M.W., Chen, C.M., Schreiber, S.L. & Walsh, C.T. (1990). Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis. Proc. Natl. Acad. Sci. USA 87, 2304-2308.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2304-2308
    • Liu, J.1    Albers, M.W.2    Chen, C.M.3    Schreiber, S.L.4    Walsh, C.T.5
  • 46
    • 84920325457 scopus 로고
    • AMoRe, an automated package for molecule replacement
    • Navaza, J. (1994). AMoRe, an automated package for molecule replacement. Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 47
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 48
    • 0001797984 scopus 로고
    • (Sayer, D., ed.), Oxford University Press, UK
    • Jones, T.A. (1982). In Computational Crystallography. (Sayer, D., ed.), pp. 303-317, Oxford University Press, UK.
    • (1982) Computational Crystallography , pp. 303-317
    • Jones, T.A.1
  • 49
    • 0000732609 scopus 로고
    • GRASP: Graphic representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: graphic representation and analysis of surface properties. Biophys. J. 64, 166-170.
    • (1993) Biophys. J. , vol.64 , pp. 166-170
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 50
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 51
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M. (1994). Raster3D version 2.0 - a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
    • (1994) Acta Cryst. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.2


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