메뉴 건너뛰기




Volumn 23, Issue 17, 2004, Pages 3441-3451

Crystal structure of the nuclear effector of Notch signaling, CSL, bound to DNA

Author keywords

Beta trefoil domain; Lag 1; RAM domain; Rel homology region; Transcription factor

Indexed keywords

DNA; NOTCH RECEPTOR; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR CSL; TRANSCRIPTION FACTOR REL; UNCLASSIFIED DRUG;

EID: 4644317278     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600349     Document Type: Article
Times cited : (133)

References (47)
  • 1
    • 0033617522 scopus 로고    scopus 로고
    • Notch signaling: Cell fate control and signal integration in development
    • Artavanis-Tsakonas S, Rand MD, Lake RJ (1999) Notch signaling: cell fate control and signal integration in development. Science 284: 770-776
    • (1999) Science , vol.284 , pp. 770-776
    • Artavanis-Tsakonas, S.1    Rand, M.D.2    Lake, R.J.3
  • 3
    • 0032485391 scopus 로고    scopus 로고
    • Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA
    • Chen L, Glover JN, Hogan PG, Rao A, Harrison SC (1998) Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA. Nature 392: 42-48
    • (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
    • 0028088509 scopus 로고
    • Site-directed mutagenesis study on DNA binding regions of the mouse homologue of Suppressor of Hairless, RBP-J kappa
    • Chung CN, Hamaguchi Y, Honjo T, Kawaichi M (1994) Site-directed mutagenesis study on DNA binding regions of the mouse homologue of Suppressor of Hairless, RBP-J kappa. Nucleic Acids Res 22: 2938-2944
    • (1994) Nucleic Acids Res , vol.22 , pp. 2938-2944
    • Chung, C.N.1    Hamaguchi, Y.2    Honjo, T.3    Kawaichi, M.4
  • 6
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • delaFortelle E, Bricogne G (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol 276: 472-494
    • (1997) Methods Enzymol , vol.276 , pp. 472-494
    • DelaFortelle, E.1    Bricogne, G.2
  • 7
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie S (1997) Preparation of selenomethionyl proteins for phase determination. Methods Enzymol 276: 523-530
    • (1997) Methods Enzymol , vol.276 , pp. 523-530
    • Doublie, S.1
  • 8
    • 0030003963 scopus 로고    scopus 로고
    • Propeller-twisting of base-pairs and the conformational mobility of dinucleotide steps in DNA
    • el Hassan MA, Calladine CR (1996) Propeller-twisting of base-pairs and the conformational mobility of dinucleotide steps in DNA. J Mol Biol 259: 95-103
    • (1996) J Mol Biol , vol.259 , pp. 95-103
    • El Hassan, M.A.1    Calladine, C.R.2
  • 9
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf RM (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 15: 132-134
    • (1997) J Mol Graph Model , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 10
    • 0038243196 scopus 로고    scopus 로고
    • POVScript +: A program for model and data visualization using persistence of vision raytracing
    • Fenn TD, Ringe D, Petsko GA (2003) POVScript +: a program for model and data visualization using persistence of vision raytracing. J Appl Crystallogr 36: 944-947
    • (2003) J Appl Crystallogr , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 11
    • 0035724485 scopus 로고    scopus 로고
    • Mutational analysis of the J recombination signal sequence binding protein (RBP-J)/Epstein-Barr virus nuclear antigen 2 (EBNA2) and RBP-J/Notch interaction
    • Fuchs KP, Bommer G, Dumont E, Christoph B, Vidal M, Kremmer E, Kempkes B (2001) Mutational analysis of the J recombination signal sequence binding protein (RBP-J)/Epstein-Barr virus nuclear antigen 2 (EBNA2) and RBP-J/Notch interaction. Eur J Biochem 268: 4639-4646
    • (2001) Eur J Biochem , vol.268 , pp. 4639-4646
    • Fuchs, K.P.1    Bommer, G.2    Dumont, E.3    Christoph, B.4    Vidal, M.5    Kremmer, E.6    Kempkes, B.7
  • 12
    • 0028979479 scopus 로고
    • Structure of NF-kappa B p50 homodimer bound to a kappa B site
    • Ghosh G, van Duyne G, Ghosh S, Sigler PB (1995) Structure of NF-kappa B p50 homodimer bound to a kappa B site. Nature 373: 303-310
    • (1995) Nature , vol.373 , pp. 303-310
    • Ghosh, G.1    Van Duyne, G.2    Ghosh, S.3    Sigler, P.B.4
  • 13
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 15
    • 0032525964 scopus 로고    scopus 로고
    • LIN-12/Notch signaling: Lessons from worms and flies
    • Greenwald I (1998) LIN-12/Notch signaling: lessons from worms and flies. Genes Dev 12: 1751-1762
    • (1998) Genes Dev , vol.12 , pp. 1751-1762
    • Greenwald, I.1
  • 16
    • 0037390535 scopus 로고    scopus 로고
    • Notch signaling and inherited disease syndromes
    • Gridley T (2003) Notch signaling and inherited disease syndromes. Hum Mol Genet 12 (Spec no. 1): R9-R13
    • (2003) Hum Mol Genet , vol.12 , Issue.SPEC. NO. 1
    • Gridley, T.1
  • 17
    • 0028133036 scopus 로고
    • Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa
    • Henkel T, Ling PD, Hayward SD, Peterson MG (1994) Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa. Science 265: 92-95
    • (1994) Science , vol.265 , pp. 92-95
    • Henkel, T.1    Ling, P.D.2    Hayward, S.D.3    Peterson, M.G.4
  • 18
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233: 123-138
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 19
    • 0028988990 scopus 로고
    • Masking of the CBF1/RBPJ kappa transcriptional repression domain by Epstein-Barr virus EBNA2
    • Hsieh JJ, Hayward SD (1995) Masking of the CBF1/RBPJ kappa transcriptional repression domain by Epstein-Barr virus EBNA2. Science 268: 560-563
    • (1995) Science , vol.268 , pp. 560-563
    • Hsieh, J.J.1    Hayward, S.D.2
  • 20
    • 0033524444 scopus 로고    scopus 로고
    • CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex
    • Hsieh JJ, Zhou S, Chen L, Young DB, Hayward SD (1999) CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex. Proc Natl Acad Sci USA 96: 23-28
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 23-28
    • Hsieh, J.J.1    Zhou, S.2    Chen, L.3    Young, D.B.4    Hayward, S.D.5
  • 21
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones TA, Kjeldgaard M (1997) Electron-density map interpretation. Methods Enzymol 277: 173-208
    • (1997) Methods Enzymol , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 22
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 24
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ (1991) Molscript - a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24: 946-950
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
  • 26
    • 0028855281 scopus 로고
    • Contribution of conserved amino acids in mediating the interaction between EBNA2 and CBF1/RBPJk
    • Ling PD, Hayward SD (1995) Contribution of conserved amino acids in mediating the interaction between EBNA2 and CBF1/RBPJk. J Virol 69: 1944-1950
    • (1995) J Virol , vol.69 , pp. 1944-1950
    • Ling, P.D.1    Hayward, S.D.2
  • 27
    • 0027358873 scopus 로고
    • The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein
    • Ling PD, Rawlins DR, Hayward SD (1993) The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein. Proc Natl Acad Sci USA 90: 9237-9241
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9237-9241
    • Ling, P.D.1    Rawlins, D.R.2    Hayward, S.D.3
  • 28
    • 0242396923 scopus 로고    scopus 로고
    • 3DNA: A software package for the analysis, rebuilding and visualization of three-dimensional nucleic acid structures
    • Lu XJ, Olson WK (2003) 3DNA: a software package for the analysis, rebuilding and visualization of three-dimensional nucleic acid structures. Nucleic Acids Res 31: 5108-5121
    • (2003) Nucleic Acids Res , vol.31 , pp. 5108-5121
    • Lu, X.J.1    Olson, W.K.2
  • 29
    • 0042286558 scopus 로고    scopus 로고
    • Notch and cancer: Best to avoid the ups and downs
    • Maillard I, Pear WS (2003) Notch and cancer: best to avoid the ups and downs. Cancer Cell 3: 203-205
    • (2003) Cancer Cell , vol.3 , pp. 203-205
    • Maillard, I.1    Pear, W.S.2
  • 31
    • 0034671686 scopus 로고    scopus 로고
    • Notch signaling: From the outside in
    • Mumm JS, Kopan R (2000) Notch signaling: from the outside in. Dev Biol 228: 151-165
    • (2000) Dev Biol , vol.228 , pp. 151-165
    • Mumm, J.S.1    Kopan, R.2
  • 32
    • 0026556882 scopus 로고
    • beta-trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors
    • Murzin AG, Lesk AM, Chothia C (1992) beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors. J Mol Biol 223: 531-543
    • (1992) J Mol Biol , vol.223 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 33
    • 0038079817 scopus 로고    scopus 로고
    • Structural requirements for assembly of the CSL intracellular Notch1. Mastermind-like 1 transcriptional activation complex
    • Nam Y, Weng AP, Aster JC, Blacklow SC (2003) Structural requirements for assembly of the CSL intracellular Notch1. Mastermind-like 1 transcriptional activation complex. J Biol Chem 278: 21232-21239
    • (2003) J Biol Chem , vol.278 , pp. 21232-21239
    • Nam, Y.1    Weng, A.P.2    Aster, J.C.3    Blacklow, S.C.4
  • 34
    • 0033198359 scopus 로고    scopus 로고
    • Discrete enhancer elements mediate selective responsiveness of enhancer of split complex genes to common transcriptional activators
    • Nellesen DT, Lai EC, Posakony JW (1999) Discrete enhancer elements mediate selective responsiveness of enhancer of split complex genes to common transcriptional activators. Dev Biol 213: 33-53
    • (1999) Dev Biol , vol.213 , pp. 33-53
    • Nellesen, D.T.1    Lai, E.C.2    Posakony, J.W.3
  • 35
    • 0023513912 scopus 로고
    • The structure of an oligo(dA).oligo(dT) tract and its biological implications
    • Nelson HC, Finch JT, Luisi BF, Klug A (1987) The structure of an oligo(dA).oligo(dT) tract and its biological implications. Nature 330: 221-226
    • (1987) Nature , vol.330 , pp. 221-226
    • Nelson, H.C.1    Finch, J.T.2    Luisi, B.F.3    Klug, A.4
  • 36
    • 0000732609 scopus 로고
    • Grasp - Graphical representation and analysis of surface-properties
    • Nicholls A, Bharadwaj R, Honig B (1993) Grasp - graphical representation and analysis of surface-properties. Biophys J 64: A166-A166
    • (1993) Biophys J , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6: 458-463
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 39
    • 0030477188 scopus 로고    scopus 로고
    • Roles of the RAM and ANK domains in signaling by the C. elegans GLP-1 receptor
    • Roehl H, Bosenberg M, Blelloch R, Kimble J (1996) Roles of the RAM and ANK domains in signaling by the C. elegans GLP-1 receptor. EMBO J 15: 7002-7012
    • (1996) EMBO J , vol.15 , pp. 7002-7012
    • Roehl, H.1    Bosenberg, M.2    Blelloch, R.3    Kimble, J.4
  • 41
    • 0029583607 scopus 로고
    • Physical interaction between a novel domain of the receptor Notch and the transcription factor RBP-J kappa/Su(H)
    • Tamura K, Taniguchi Y, Minoguchi S, Sakai T, Tun T, Furukawa T, Honjo T (1995) Physical interaction between a novel domain of the receptor Notch and the transcription factor RBP-J kappa/Su(H). Curr Biol 5: 1416-1423
    • (1995) Curr Biol , vol.5 , pp. 1416-1423
    • Tamura, K.1    Taniguchi, Y.2    Minoguchi, S.3    Sakai, T.4    Tun, T.5    Furukawa, T.6    Honjo, T.7
  • 42
    • 0035369630 scopus 로고    scopus 로고
    • Identification of a novel activation domain in the Notch-responsive transcription factor CSL
    • Tang Z, Kadesch T (2001) Identification of a novel activation domain in the Notch-responsive transcription factor CSL. Nucleic Acids Res 29: 2284-2291
    • (2001) Nucleic Acids Res , vol.29 , pp. 2284-2291
    • Tang, Z.1    Kadesch, T.2
  • 43
    • 0035869115 scopus 로고    scopus 로고
    • The N- and C-terminal regions of RBP-J interact with the ankyrin repeats of Notchl RAMIC to activate transcription
    • Tani S, Kurooka H, Aoki T, Hashimoto N, Honjo T (2001) The N- and C-terminal regions of RBP-J interact with the ankyrin repeats of Notchl RAMIC to activate transcription. Nucleic Acids Res 29: 1373-1380
    • (2001) Nucleic Acids Res , vol.29 , pp. 1373-1380
    • Tani, S.1    Kurooka, H.2    Aoki, T.3    Hashimoto, N.4    Honjo, T.5
  • 45
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 47
    • 0034073379 scopus 로고    scopus 로고
    • SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC to facilitate NotchIC function
    • Zhou S, Fujimuro M, Hsieh JJ, Chen L, Miyamoto A, Weinmaster G, Hayward SD (2000) SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC to facilitate NotchIC function. Mol Cell Biol 20: 2400-2410
    • (2000) Mol Cell Biol , vol.20 , pp. 2400-2410
    • Zhou, S.1    Fujimuro, M.2    Hsieh, J.J.3    Chen, L.4    Miyamoto, A.5    Weinmaster, G.6    Hayward, S.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.