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Volumn 10, Issue 10, 2003, Pages 800-806

Structure of NFAT1 bound as a dimer to the HIV-1 LTR κB element

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MONOMER; TRANSCRIPTION FACTOR NFAT; TRANSCRIPTION FACTOR NFAT1; TRANSCRIPTION FACTOR NFAT5; UNCLASSIFIED DRUG;

EID: 0141841774     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb981     Document Type: Article
Times cited : (94)

References (46)
  • 1
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao, A., Luo, C. & Hogan, P.G. Transcription factors of the NFAT family: regulation and function. Annu. Rev. Immunol. 15, 707-747 (1997).
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 2
    • 0036234543 scopus 로고    scopus 로고
    • NFAT signaling: Choreographing the social lives of cells
    • Crabtree, G.R. & Olson, E.N. NFAT signaling: choreographing the social lives of cells. Cell 109 (suppl.), S67-S79 (2002).
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Crabtree, G.R.1    Olson, E.N.2
  • 3
    • 0028361589 scopus 로고
    • NF-AT components define a family of transcription factors targeted in T-cell activation
    • Northrop, J.P. et al. NF-AT components define a family of transcription factors targeted in T-cell activation. Nature 369, 497-502 (1994).
    • (1994) Nature , vol.369 , pp. 497-502
    • Northrop, J.P.1
  • 4
    • 0032485391 scopus 로고    scopus 로고
    • Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA
    • Chen, L., Glover, J.N., Hogan, P.G., Rao, A. & Harrison, S.C. Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA. Nature 392, 42-48 (1998).
    • (1998) Nature , vol.392 , pp. 42-48
    • Chen, L.1    Glover, J.N.2    Hogan, P.G.3    Rao, A.4    Harrison, S.C.5
  • 5
    • 0028979479 scopus 로고
    • Structure of NF-κB p50 homodimer bound to a κB site
    • Ghosh, G., van Duyne, G., Ghosh, S. & Sigler, P.B. Structure of NF-κB p50 homodimer bound to a κB site. Nature 373, 303-310 (1995).
    • (1995) Nature , vol.373 , pp. 303-310
    • Ghosh, G.1    Van Duyne, G.2    Ghosh, S.3    Sigler, P.B.4
  • 7
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen, F.E., Huang, D.B., Chen, Y.Q. & Ghosh, G. Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature 391, 410-413 (1998).
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 8
    • 0036172880 scopus 로고    scopus 로고
    • Structure of a TonEBP-DNA complex reveals DNA encircled by a transcription factor
    • Stroud, J.C., Lopez-Rodriguez, C., Rao, A. & Chen, L. Structure of a TonEBP-DNA complex reveals DNA encircled by a transcription factor. Nat. Struct. Biol. 9, 90-94 (2002).
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 90-94
    • Stroud, J.C.1    Lopez-Rodriguez, C.2    Rao, A.3    Chen, L.4
  • 9
    • 0034907525 scopus 로고    scopus 로고
    • Bridging the NFAT and NF-κB families: NFAT 5 dimerization regulates cytokine gene transcription in response to osmotic stress
    • Lopez-Rodriguez, C. et al. Bridging the NFAT and NF-κB families: NFAT5 dimerization regulates cytokine gene transcription in response to osmotic stress. Immunity 15, 47-58 (2001).
    • (2001) Immunity , vol.15 , pp. 47-58
    • Lopez-Rodriguez, C.1
  • 10
    • 13044250453 scopus 로고    scopus 로고
    • Tonicity-responsive enhancer binding protein, a Rel-like protein that stimulates transcription in response to hypertonicity
    • Miyakawa, H., Woo, S.K., Dahl, S.C., Handler, J.S. & Kwon, H.M. Tonicity-responsive enhancer binding protein, a Rel-like protein that stimulates transcription in response to hypertonicity. Proc. Natl. Acad. Sci. USA 96, 2538-2542 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2538-2542
    • Miyakawa, H.1    Woo, S.K.2    Dahl, S.C.3    Handler, J.S.4    Kwon, H.M.5
  • 11
    • 0029346959 scopus 로고
    • Only one of the two DNA-bound orientations of AP-1 found in solution cooperates with NFATp
    • Chen, L. et al. Only one of the two DNA-bound orientations of AP-1 found in solution cooperates with NFATp. Curr. Biol. 5, 882-889 (1995).
    • (1995) Curr. Biol. , vol.5 , pp. 882-889
    • Chen, L.1
  • 12
    • 0029863521 scopus 로고    scopus 로고
    • The Rel family of eukaryotic transcription factors
    • Chytil, M. & Verdine, G.L. The Rel family of eukaryotic transcription factors. Curr. Opin. Struct. Biol. 6, 91-100 (1996).
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 91-100
    • Chytil, M.1    Verdine, G.L.2
  • 13
    • 0029053852 scopus 로고
    • Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins
    • Hoey, T., Sun, Y.L., Williamson, K. & Xu, X. Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins. Immunity 2, 461-472 (1995).
    • (1995) Immunity , vol.2 , pp. 461-472
    • Hoey, T.1    Sun, Y.L.2    Williamson, K.3    Xu, X.4
  • 14
    • 0028073754 scopus 로고
    • The role of NFATp in cyclosporin A-sensitive tumor necrosis factor-α gene transcription
    • McCaffrey, P.G., Goldfeld, A.E. & Rao, A. The role of NFATp in cyclosporin A-sensitive tumor necrosis factor-α gene transcription. J. Biol. Chem. 269, 30445-30450 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 30445-30450
    • McCaffrey, P.G.1    Goldfeld, A.E.2    Rao, A.3
  • 15
    • 0032848185 scopus 로고    scopus 로고
    • Combinatorial gene regulation by eukaryotic transcription factors
    • Chen, L. Combinatorial gene regulation by eukaryotic transcription factors. Curr. Opin. Struct. Biol. 9, 48-55 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 48-55
    • Chen, L.1
  • 16
    • 0034283018 scopus 로고    scopus 로고
    • Gene expression elicited by NFAT in the presence or absence of cooperative recruitment of Fos and Jun
    • Macian, F., Garcia-Rodriguez, C. & Rao, A. Gene expression elicited by NFAT in the presence or absence of cooperative recruitment of Fos and Jun. EMBO J. 19, 4783-4795 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4783-4795
    • Macian, F.1    Garcia-Rodriguez, C.2    Rao, A.3
  • 17
    • 0037077135 scopus 로고    scopus 로고
    • Transcriptional mechanisms underlying lymphocyte tolerance
    • Macian, F. et al. Transcriptional mechanisms underlying lymphocyte tolerance. Cell 109, 719-731 (2002).
    • (2002) Cell , vol.109 , pp. 719-731
    • Macian, F.1
  • 18
    • 0030939152 scopus 로고    scopus 로고
    • The T cell activation factor NF-ATc positively regulates HIV-1 replication and gene expression in T cells
    • Kinoshita, S. et al. The T cell activation factor NF-ATc positively regulates HIV-1 replication and gene expression in T cells. Immunity 6, 235-44 (1997).
    • (1997) Immunity , vol.6 , pp. 235-244
    • Kinoshita, S.1
  • 19
    • 0032567042 scopus 로고    scopus 로고
    • Host control of HIV-1 parasitism in T cells by the nuclear factor of activated T cells
    • Kinoshita, S., Chen, B.K., Kaneshima, H. & Nolan, G.P. Host control of HIV-1 parasitism in T cells by the nuclear factor of activated T cells. Cell 95, 595-604 (1998).
    • (1998) Cell , vol.95 , pp. 595-604
    • Kinoshita, S.1    Chen, B.K.2    Kaneshima, H.3    Nolan, G.P.4
  • 20
    • 0034011644 scopus 로고    scopus 로고
    • NFAT1 enhances HIV-1 gene expression in primary human CD4 T cells
    • Cron, R.Q. et al. NFAT1 enhances HIV-1 gene expression in primary human CD4 T cells. Clin. Immunol. 94, 179-191 (2000).
    • (2000) Clin. Immunol. , vol.94 , pp. 179-191
    • Cron, R.Q.1
  • 22
    • 0030610544 scopus 로고    scopus 로고
    • The κB sites in the human immunodeficiency virus type 1 long terminal repeat enhance virus replication yet are not absolutely required for viral growth
    • Chen, B.K., Feinberg, M.B. & Baltimore, D. The κB sites in the human immunodeficiency virus type 1 long terminal repeat enhance virus replication yet are not absolutely required for viral growth. J. Virol. 71, 5495-5504 (1997).
    • (1997) J. Virol. , vol.71 , pp. 5495-5504
    • Chen, B.K.1    Feinberg, M.B.2    Baltimore, D.3
  • 23
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκBα/NF-κB complex
    • Jacobs, M.D. & Harrison, S.C. Structure of an IκBα /NF-κB complex. Cell 95, 749-758 (1998).
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 24
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation
    • Huxford, T., Huang, D.B., Malek, S. & Ghosh, G. The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation. Cell 95, 759-770 (1998).
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 25
    • 0141507041 scopus 로고    scopus 로고
    • An asymmetric NFAT1 dimer on a pseudo-palindromic κB-like DNA site
    • advance online publication, 31 August (doi:10.1038/nsb 975)
    • Jin, L. et al. An asymmetric NFAT1 dimer on a pseudo-palindromic κB-like DNA site. Nat. Struct. Biol. advance online publication, 31 August 2003 (doi:10.1038/nsb975).
    • (2003) Nat. Struct. Biol.
    • Jin, L.1
  • 26
    • 0037187073 scopus 로고    scopus 로고
    • Molecular mechanism of NFAT family proteins for differential regulation of the IL-2 and TNF-α promoters
    • Oum, J.H. et al. Molecular mechanism of NFAT family proteins for differential regulation of the IL-2 and TNF-α promoters. Mol. Cell 13, 77-84 (2002).
    • (2002) Mol. Cell , vol.13 , pp. 77-84
    • Oum, J.H.1
  • 27
    • 0026601673 scopus 로고
    • A T cell nuclear factor resembling NF-AT binds to an NF-κB site and to the conserved lymphokine promoter sequence 'cytokine-1'
    • McCaffrey, P.G., Jain, J., Jamieson, C., Sen, R. & Rao, A. A T cell nuclear factor resembling NF-AT binds to an NF-κB site and to the conserved lymphokine promoter sequence 'cytokine-1'. J. Biol. Chem. 267, 1864-1871 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 1864-1871
    • McCaffrey, P.G.1    Jain, J.2    Jamieson, C.3    Sen, R.4    Rao, A.5
  • 28
    • 0031964687 scopus 로고    scopus 로고
    • A novel DNA recognition mode by the NF-κB p65 homodimer
    • Chen, Y.Q., Ghosh, S. & Ghosh, G. A novel DNA recognition mode by the NF-κB p65 homodimer. Nat. Struct. Biol. 5, 67-73 (1998).
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 67-73
    • Chen, Y.Q.1    Ghosh, S.2    Ghosh, G.3
  • 29
    • 0034634340 scopus 로고    scopus 로고
    • Allosteric effects of Pit-1 DNA sites on long-term repression in cell type specification
    • Scully, K.M. et al. Allosteric effects of Pit-1 DNA sites on long-term repression in cell type specification. Science 290, 1127-1131 (2000).
    • (2000) Science , vol.290 , pp. 1127-1131
    • Scully, K.M.1
  • 30
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin, J.A. & Yamamoto, K.R. Allosteric effects of DNA on transcriptional regulators. Nature 392, 885-888 (1998).
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 31
    • 0036124647 scopus 로고    scopus 로고
    • Structure of NF-κB p50/p65 heterodimer bound to the PRDII DNA element from the interferon-β promoter
    • Escalante, C.R., Shen, L., Thanos, D. & Aggarwal, A.K. Structure of NF-κB p50/p65 heterodimer bound to the PRDII DNA element from the interferon-β promoter. Structure 10, 383-391 (2002).
    • (2002) Structure , vol.10 , pp. 383-391
    • Escalante, C.R.1    Shen, L.2    Thanos, D.3    Aggarwal, A.K.4
  • 32
    • 0022481133 scopus 로고
    • Multiple nuclear factors interact with the immunoglobulin enhancer sequences
    • Sen, R. & Baltimore, D. Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 46, 705-716 (1986).
    • (1986) Cell , vol.46 , pp. 705-716
    • Sen, R.1    Baltimore, D.2
  • 33
    • 0023176085 scopus 로고
    • An inducible transcription factor activates expression of human immunodeficiency virus in T cells
    • Nabel, G. & Baltimore, D. An inducible transcription factor activates expression of human immunodeficiency virus in T cells. Nature 326, 711-713 (1987).
    • (1987) Nature , vol.326 , pp. 711-713
    • Nabel, G.1    Baltimore, D.2
  • 34
    • 0027326457 scopus 로고
    • Identification of a novel cyclosporin-sensitive element in the human tumor necrosis factor-α gene promoter
    • Goldfeld, A.E., McCaffrey, P.G., Strominger, J.L. & Rao, A. Identification of a novel cyclosporin-sensitive element in the human tumor necrosis factor-α gene promoter. J. Exp. Med. 178, 1365-1379 (1993).
    • (1993) J. Exp. Med. , vol.178 , pp. 1365-1379
    • Goldfeld, A.E.1    McCaffrey, P.G.2    Strominger, J.L.3    Rao, A.4
  • 35
    • 0028176449 scopus 로고
    • The interleukin-8 AP-1 and κB-like sites are genetic end targets of FK506-sensitive pathway accompanied by calcium mobilization
    • Okamoto, S. et al. The interleukin-8 AP-1 and κB-like sites are genetic end targets of FK506-sensitive pathway accompanied by calcium mobilization. J. Biol. Chem. 269, 8582-8589 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 8582-8589
    • Okamoto, S.1
  • 36
    • 0032489431 scopus 로고    scopus 로고
    • Solution structure of the core NFATC1/DNA complex
    • Zhou, P., Sun, L.J., Dotsch, V., Wagner, G. & Verdine, G.L. Solution structure of the core NFATC1/DNA complex. Cell 92, 687-696 (1998).
    • (1998) Cell , vol.92 , pp. 687-696
    • Zhou, P.1    Sun, L.J.2    Dotsch, V.3    Wagner, G.4    Verdine, G.L.5
  • 37
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506
    • Schreiber, S.L. & Crabtree, G.R. The mechanism of action of cyclosporin A and FK506. Immunol. Today 13, 136-142 (1992).
    • (1992) Immunol Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 38
    • 0032540267 scopus 로고    scopus 로고
    • A calcineurin-dependent transcriptional pathway for cardiac hypertrophy
    • Molkentin, J.D. et al. A calcineurin-dependent transcriptional pathway for cardiac hypertrophy. Cell 93, 215-228 (1998).
    • (1998) Cell , vol.93 , pp. 215-228
    • Molkentin, J.D.1
  • 39
    • 0033698581 scopus 로고    scopus 로고
    • Manipulating immune responses with immunosuppressive agents that target NFAT
    • Kiani, A., Rao, A. & Aramburu, J. Manipulating immune responses with immunosuppressive agents that target NFAT. Immunity 12, 359-372 (2000).
    • (2000) Immunity , vol.12 , pp. 359-372
    • Kiani, A.1    Rao, A.2    Aramburu, J.3
  • 40
    • 0032849010 scopus 로고    scopus 로고
    • Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A
    • Aramburu, J. et al. Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A. Science 285, 2129-2133 (1999).
    • (1999) Science , vol.285 , pp. 2129-2133
    • Aramburu, J.1
  • 41
    • 0002452464 scopus 로고
    • (eds. Sawyer, L., Isaacs, N. & Burley, S.) (Daresbury Laboratories, Warrington, UK
    • Otwinowski, Z. In Proceedings of the CCP4 Study Weekend (eds. Sawyer, L., Isaacs, N. & Burley, S.) 56-62 (Daresbury Laboratories, Warrington, UK, (1993).
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 42
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. A 54, 905-921 (1998).
    • (1998) Acta Crystallogr. A , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 43
    • 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. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (Pt. 2), 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 44
    • 0028103275 scopus 로고
    • CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. CCP4 Suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 46
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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