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Volumn 76, Issue 2-3, 1998, Pages 368-378

New perceptions of transcription factor properties from NMR

Author keywords

Conformational fluctuations; Induced folding; Protein DNA interaction; Protein protein interaction; Transcriptional regulation

Indexed keywords

DNA; HOMEODOMAIN PROTEIN; RNA POLYMERASE II; TATA BINDING PROTEIN; TRANSCRIPTION FACTOR; WATER;

EID: 0032468814     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o98-064     Document Type: Review
Times cited : (7)

References (85)
  • 1
    • 0026015213 scopus 로고
    • The solution structures of Escherichia coli Trp represser and Trp aporepressor at an intermediate resolution
    • Arrowsmith, C., Pachter, R., Altman, R., and Jardetzky, O. 1991. The solution structures of Escherichia coli Trp represser and Trp aporepressor at an intermediate resolution. Eur. J. Biochem. 202: 53-66.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 53-66
    • Arrowsmith, C.1    Pachter, R.2    Altman, R.3    Jardetzky, O.4
  • 2
    • 0029120954 scopus 로고
    • Solution structure of the C-terminal core domain of human TFIIB: Similarity to cyclin A and interaction with TATA-binding protein
    • Bagby, S., Kim, S., Maldonado, E., Tong, K.I., Reinberg, D., and Ikura, M. 1995. Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein. Cell, 82: 857-867.
    • (1995) Cell , vol.82 , pp. 857-867
    • Bagby, S.1    Kim, S.2    Maldonado, E.3    Tong, K.I.4    Reinberg, D.5    Ikura, M.6
  • 6
    • 0027787519 scopus 로고
    • Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex
    • Billeter, M., Qian, Y.Q., Otting, G., Müller, M., Gehring, W., and Wüthrich, K. 1993. Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex. J. Mol. Biol. 234: 1084-1097.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1084-1097
    • Billeter, M.1    Qian, Y.Q.2    Otting, G.3    Müller, M.4    Gehring, W.5    Wüthrich, K.6
  • 7
    • 0030604702 scopus 로고
    • Hydration and DNA recognition by homeodomains
    • Billeter, M., Güntert, P., Luginbühl, P., and Wüthrich, K. 1995. Hydration and DNA recognition by homeodomains. Cell, 85: 1057-1065.
    • (1995) Cell , vol.85 , pp. 1057-1065
    • Billeter, M.1    Güntert, P.2    Luginbühl, P.3    Wüthrich, K.4
  • 8
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • Brüschweiler, R., Liao, X., and Wright, P.E. 1995. Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science (Washington, D.C.), 268: 886-889.
    • (1995) Science (Washington, D.C.) , vol.268 , pp. 886-889
    • Brüschweiler, R.1    Liao, X.2    Wright, P.E.3
  • 11
    • 0030039788 scopus 로고    scopus 로고
    • Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy
    • Cho, H.S., Liu, C.W., Damberger, F.F., Pelton, J.G., Nelson, H.C., and Wemmer, D.E. 1996. Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. Protein Sci. 5: 262-269.
    • (1996) Protein Sci. , vol.5 , pp. 262-269
    • Cho, H.S.1    Liu, C.W.2    Damberger, F.F.3    Pelton, J.G.4    Nelson, H.C.5    Wemmer, D.E.6
  • 12
    • 0027426159 scopus 로고
    • Structure of the complex of lac repressor headpiece and an 11 base-pair half-operator by nuclear magnetic resonance spectroscopy and restrained molecular dynamics
    • Chuprina, V.P., Rullmann, J.A.C., Lamerichs, R.M.J.N., van Boom, J.H., Boelens, R., and Kaptein, R. 1993. Structure of the complex of lac repressor headpiece and an 11 base-pair half-operator by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. J. Mol. Biol. 234: 446-462.
    • (1993) J. Mol. Biol. , vol.234 , pp. 446-462
    • Chuprina, V.P.1    Rullmann, J.A.C.2    Lamerichs, R.M.J.N.3    Van Boom, J.H.4    Boelens, R.5    Kaptein, R.6
  • 14
    • 0028871798 scopus 로고
    • Side-chain conformational entropy in protein folding
    • Doig, A.J., and Sternberg, M.J.E. 1995. Side-chain conformational entropy in protein folding. Protein Sci. 4: 2247-2251.
    • (1995) Protein Sci. , vol.4 , pp. 2247-2251
    • Doig, A.J.1    Sternberg, M.J.E.2
  • 15
    • 0026540830 scopus 로고
    • Purification and characterization of the carboxy-terminal transactivation domain of Vmw65 from herpes simplex virus type 1
    • Donaldson, L., and Capone, J.P. 1992. Purification and characterization of the carboxy-terminal transactivation domain of Vmw65 from herpes simplex virus type 1. J. Biol. Chem. 267: 1411-1414.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1411-1414
    • Donaldson, L.1    Capone, J.P.2
  • 16
    • 0030044420 scopus 로고    scopus 로고
    • Solution structure of the ETS domain from murine Ets-1: A winged helix-turn-helix DNA binding motif
    • Donaldson, L.J., Petersen, J.M., Graves, B.J., and McIntosh, L.P. 1996. Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motif. EMBO J. 15: 125-134.
    • (1996) EMBO J. , vol.15 , pp. 125-134
    • Donaldson, L.J.1    Petersen, J.M.2    Graves, B.J.3    McIntosh, L.P.4
  • 17
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: Crystal structure of the protein-DNA complex
    • Ellenberger, T.E., Brandl, C.J., Struhl, K., and Harrison, S.C. 1992. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex. Cell, 71: 1223-1237.
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandl, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 18
    • 0027749348 scopus 로고
    • The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition
    • Fairall, L., Schwabe, J.W.R., Chapman, L., Finch, J.T., and Rhodes, D. 1993. The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition. Nature (London), 366: 483-487.
    • (1993) Nature (London) , vol.366 , pp. 483-487
    • Fairall, L.1    Schwabe, J.W.R.2    Chapman, L.3    Finch, J.T.4    Rhodes, D.5
  • 21
    • 0021710076 scopus 로고
    • Xenopus 5S gene transcription factor, TFIIIA: Characterization of a cDNA clone and measurement of RNA levels throughout development
    • Ginsberg, A.M., King, B.O., and Roeder, R.G. 1984. Xenopus 5S gene transcription factor, TFIIIA: characterization of a cDNA clone and measurement of RNA levels throughout development. Cell, 39: 479-489.
    • (1984) Cell , vol.39 , pp. 479-489
    • Ginsberg, A.M.1    King, B.O.2    Roeder, R.G.3
  • 22
    • 0028894384 scopus 로고
    • The crystal structure of the heterodimeric bZip transcription factor cFos:cJun bound to DNA
    • Glover, J.N.M., and Harrison, S.C. 1994. The crystal structure of the heterodimeric bZip transcription factor cFos:cJun bound to DNA. Nature (London), 373: 257-261.
    • (1994) Nature (London) , vol.373 , pp. 257-261
    • Glover, J.N.M.1    Harrison, S.C.2
  • 23
    • 0032512852 scopus 로고    scopus 로고
    • Inner workings of a transcription factor partnership
    • Graves, B.J. 1998. Inner workings of a transcription factor partnership. Science (Washington, D.C.), 279: 1000-1002.
    • (1998) Science (Washington, D.C.) , vol.279 , pp. 1000-1002
    • Graves, B.J.1
  • 24
    • 0025820544 scopus 로고
    • Cloning of a human gene encoding the general transcription initiation factor IIB
    • Ha, I., Lane, W.S., and Reinberg, D. 1991. Cloning of a human gene encoding the general transcription initiation factor IIB. Nature (London), 352: 689-695.
    • (1991) Nature (London) , vol.352 , pp. 689-695
    • Ha, I.1    Lane, W.S.2    Reinberg, D.3
  • 26
    • 0032474445 scopus 로고    scopus 로고
    • Human general transcription factor TFIIB: Conformational variability and interaction with VP16 activation domain
    • Hayashi, F., Ishima, R., Liu, D., Tong, K.I., Kim, S., Reinberg, D., Bagby, S., and Ikura, M. 1998. Human general transcription factor TFIIB: conformational variability and interaction with VP16 activation domain. Biochemistry, 37: 7941-7951.
    • (1998) Biochemistry , vol.37 , pp. 7941-7951
    • Hayashi, F.1    Ishima, R.2    Liu, D.3    Tong, K.I.4    Kim, S.5    Reinberg, D.6    Bagby, S.7    Ikura, M.8
  • 27
    • 0029595248 scopus 로고
    • Structure of the even-skipped homeodomain complexed to AT-rich DNA: New perspectives on homeodomain specificity
    • Hirsch, J.A., and Aggarwal, A.K. 1995. Structure of the even-skipped homeodomain complexed to AT-rich DNA: new perspectives on homeodomain specificity. EMBO J. 14: 6280-6291.
    • (1995) EMBO J. , vol.14 , pp. 6280-6291
    • Hirsch, J.A.1    Aggarwal, A.K.2
  • 29
    • 0025188837 scopus 로고
    • Crystal structure of an engrailed homeodomain/DNA complex at 2.8 Å resolution: A framework for understanding homeodomain/DNA interactions
    • Kissinger, C.R., Liu, B., Martin-Blanco, E., Kornberg, T.B., and Pabo, C.O. 1990. Crystal structure of an engrailed homeodomain/DNA complex at 2.8 Å resolution: a framework for understanding homeodomain/DNA interactions. Cell, 63: 579-590.
    • (1990) Cell , vol.63 , pp. 579-590
    • Kissinger, C.R.1    Liu, B.2    Martin-Blanco, E.3    Kornberg, T.B.4    Pabo, C.O.5
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. 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.1
  • 33
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin, J., and Yamamoto, K.R. 1998. Allosteric effects of DNA on transcriptional regulators. Nature (London), 392: 885-888.
    • (1998) Nature (London) , vol.392 , pp. 885-888
    • Lefstin, J.1    Yamamoto, K.R.2
  • 34
    • 0028116117 scopus 로고
    • Structural and functional analysis of the NF-kappa B p65 C-terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation
    • Lienhard Schmitz, M., dos Santos Silva, M., Altmann, H., Czisch, M., Holak, T., and Baeuerle, P.A. 1994. Structural and functional analysis of the NF-kappa B p65 C-terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation. J. Biol. Chem. 269: 25 613-25 620.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25613-25620
    • Lienhard Schmitz, M.1    Dos Santos Silva, M.2    Altmann, H.3    Czisch, M.4    Holak, T.5    Baeuerle, P.A.6
  • 36
    • 0029131298 scopus 로고
    • Structural basis for DNA bending by the architectural transcription factor LEF-1
    • Love, J.J., Li, X., Case, D.A., Giese, K., Grosschedl, R., and Wright, P.E. 1995. Structural basis for DNA bending by the architectural transcription factor LEF-1. Nature (London), 376: 791-795.
    • (1995) Nature (London) , vol.376 , pp. 791-795
    • Love, J.J.1    Li, X.2    Case, D.A.3    Giese, K.4    Grosschedl, R.5    Wright, P.E.6
  • 38
    • 0025936684 scopus 로고
    • Sequence of general transcription factor TFIIB and relationships to other initiation factors
    • Malik, S., Hisatake, K., Sumimoto, H., Horikoshi, M., and Roeder, R.G. 1991. Sequence of general transcription factor TFIIB and relationships to other initiation factors. Proc. Natl. Acad. Sci. U.S.A. 88: 9553-9557.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9553-9557
    • Malik, S.1    Hisatake, K.2    Sumimoto, H.3    Horikoshi, M.4    Roeder, R.G.5
  • 39
    • 0027445708 scopus 로고
    • Potential RNA polymerase II-induced interactions of transcription factor TFIIB
    • Malik, S., Lee, D.K., and Roeder, R.G. 1993. Potential RNA polymerase II-induced interactions of transcription factor TFIIB. Mol. Cell. Biol. 13: 6253-6259.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6253-6259
    • Malik, S.1    Lee, D.K.2    Roeder, R.G.3
  • 40
    • 0026547747 scopus 로고
    • DNA recognition by GAL4: Structure of a protein-DNA complex
    • Marmorstein, R., Carey, M., Ptashne, M., and Harrison, S.C. 1992. DNA recognition by GAL4: structure of a protein-DNA complex. Nature (London), 356: 408-414.
    • (1992) Nature (London) , vol.356 , pp. 408-414
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 41
    • 0029740873 scopus 로고    scopus 로고
    • Functional interaction of the c-Myc transactivation domain with the TATA binding protein: Evidence for an induced fit model of transactivation domain folding
    • McEwan, I.J., Dahlman-Wright, K., Ford, J., and Wright, A.P.H. 1996. Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. Biochemistry, 35: 9584-9593.
    • (1996) Biochemistry , vol.35 , pp. 9584-9593
    • McEwan, I.J.1    Dahlman-Wright, K.2    Ford, J.3    Wright, A.P.H.4
  • 42
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt, E.A., and Bacon, D.J. 1997. Raster3D photorealistic molecular graphics. Methods Enzymol. 277: 503-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 503-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 43
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller, J., McLachlan, A.D., and Klug, A. 1985. Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J. 4: 1609-1614.
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 44
    • 0029763189 scopus 로고    scopus 로고
    • Elongation factor TFIIS contains three structural domains: Solution structure of domain II
    • Morin, P., Awrey, D., Edwards, A.M., and Arrowsmith, C. 1996. Elongation factor TFIIS contains three structural domains: solution structure of domain II. Proc. Natl. Acad. Sci. U.S.A. 93: 10 604-10 608.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10604-10608
    • Morin, P.1    Awrey, D.2    Edwards, A.M.3    Arrowsmith, C.4
  • 48
    • 0028138773 scopus 로고
    • Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices
    • Ogata, K., Morikawa, S., Nakamura, H., Sekikawa, A., Inoue, T., Kanai, H., Sarai, A., Ishii, S., and Nishimura, Y. 1994. Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices. Cell, 79: 639-648.
    • (1994) Cell , vol.79 , pp. 639-648
    • Ogata, K.1    Morikawa, S.2    Nakamura, H.3    Sekikawa, A.4    Inoue, T.5    Kanai, H.6    Sarai, A.7    Ishii, S.8    Nishimura, Y.9
  • 49
    • 0032575501 scopus 로고    scopus 로고
    • Yeast transcript elongation factor TFIIS: Structure and function I. NMR structural analysis of the minimal transcriptionally active region
    • Olmsted, V., Awrey, D.E., Koth, C., Morin, P.E., Shan, X., Kazanis, S., Edwards, A.M., and Arrowsmith, C.H. 1998. Yeast transcript elongation factor TFIIS: structure and function I. NMR structural analysis of the minimal transcriptionally active region. J. Biol. Chem. 273: 22 589-22 594.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22589-22594
    • Olmsted, V.1    Awrey, D.E.2    Koth, C.3    Morin, P.E.4    Shan, X.5    Kazanis, S.6    Edwards, A.M.7    Arrowsmith, C.H.8
  • 51
  • 52
    • 0030719460 scopus 로고    scopus 로고
    • 15N chemical shifts in a protein-DNA complex resulting from magnetic ordering in solution
    • 15N chemical shifts in a protein-DNA complex resulting from magnetic ordering in solution. J. Am. Chem. Soc. 119: 9825-9830.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 9825-9830
    • Ottiger, M.1    Tjandra, N.2    Bax, A.3
  • 54
    • 0029142571 scopus 로고
    • Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain-phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches
    • Pascal, S.M., Yamazaki, T., Singer, A.U., Kay, L.E., and Forman-Kay, J.D. 1995. Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain-phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches. Biochemistry, 34: 11 353-11 362.
    • (1995) Biochemistry , vol.34 , pp. 11353-11362
    • Pascal, S.M.1    Yamazaki, T.2    Singer, A.U.3    Kay, L.E.4    Forman-Kay, J.D.5
  • 55
    • 0001578428 scopus 로고
    • Updating structure - Function relationships in the bZip family of transcription factors
    • Pathak, D., and Sigler, P.B. 1992. Updating structure - function relationships in the bZip family of transcription factors. Curr. Opin. Struct. Biol. 2: 116-123.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 116-123
    • Pathak, D.1    Sigler, P.B.2
  • 56
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å
    • Pavletich, N.P., and Pabo, C.O. 1991. Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Å. Science (Washington, D.C.), 252: 809-817.
    • (1991) Science (Washington, D.C.) , vol.252 , pp. 809-817
    • Pavletich, N.P.1    Pabo, C.O.2
  • 57
    • 0027423758 scopus 로고
    • Crystal structure of a five-finger GLI-DNA complex: New perspectives on zinc fingers
    • Pavletich, N.P., and Pabo, C.O. 1993. Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers. Science (Washington, D.C.), 261: 1701-1707.
    • (1993) Science (Washington, D.C.) , vol.261 , pp. 1701-1707
    • Pavletich, N.P.1    Pabo, C.O.2
  • 58
    • 0024407460 scopus 로고
    • The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: Comparison with prokaryotic repressors
    • Qian, Y.Q., Billeter, M., Otting, G., Müller, G., Gehring, W.J., and Wüthrich, K. 1989. The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: comparison with prokaryotic repressors. Cell, 59: 573-580.
    • (1989) Cell , vol.59 , pp. 573-580
    • Qian, Y.Q.1    Billeter, M.2    Otting, G.3    Müller, G.4    Gehring, W.J.5    Wüthrich, K.6
  • 59
    • 0027371187 scopus 로고
    • Novel zinc finger motif in the basal transcriptional machinery: Three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS
    • Qian, X., Gozani, S.N., Yoon, H., Jeon, C., Agarwal, K., and Weiss, M.A. 1993a. Novel zinc finger motif in the basal transcriptional machinery: three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS. Biochemistry, 32: 9944-9959.
    • (1993) Biochemistry , vol.32 , pp. 9944-9959
    • Qian, X.1    Gozani, S.N.2    Yoon, H.3    Jeon, C.4    Agarwal, K.5    Weiss, M.A.6
  • 60
    • 0027328862 scopus 로고
    • Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS
    • Qian, X., Jeon, C., Yoon, H., Agarwal, K., and Weiss, M. 1993b. Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS. Nature (London), 365: 277-279.
    • (1993) Nature (London) , vol.365 , pp. 277-279
    • Qian, X.1    Jeon, C.2    Yoon, H.3    Agarwal, K.4    Weiss, M.5
  • 61
    • 0000764227 scopus 로고
    • NMR detection of hydration water in the intermolecular interface of a protein -DNA complex
    • Qian, Y.Q., Otting, G., and Wüthrich, K. 1993c. NMR detection of hydration water in the intermolecular interface of a protein -DNA complex. J. Am. Chem. Soc. 115: 1189-1190.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1189-1190
    • Qian, Y.Q.1    Otting, G.2    Wüthrich, K.3
  • 62
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:Coactivator interactions
    • Radhakrishnan, I., Perez-Alvarado, G.C., Parker, D., Dyson, H.J., Montminy, M.R., and Wright, P.E. 1997. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell, 91: 741-752.
    • (1997) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Perez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 64
    • 0025865320 scopus 로고
    • Solution structure of the basic region from the transcriptional activator GCN4
    • Saudek, V., Pasley, H.S., Gibson, T., Gausepohl, H., Frank, R., and Pastore, A. 1991. Solution structure of the basic region from the transcriptional activator GCN4. Biochemistry, 30: 1310-1317.
    • (1991) Biochemistry , vol.30 , pp. 1310-1317
    • Saudek, V.1    Pasley, H.S.2    Gibson, T.3    Gausepohl, H.4    Frank, R.5    Pastore, A.6
  • 65
    • 0030596509 scopus 로고    scopus 로고
    • Refined structure of lac repressor headpiece (1-56) determined by relaxation matrix calculations from 2D and 3D NOE data: Change of tertiary structure upon binding to the lac operator
    • Slijper, M., Bonvin, A.M.J.J., Boelens, R., and Kaptein, R. 1996. Refined structure of lac repressor headpiece (1-56) determined by relaxation matrix calculations from 2D and 3D NOE data: change of tertiary structure upon binding to the lac operator. J. Mol. Biol. 259: 761-773.
    • (1996) J. Mol. Biol. , vol.259 , pp. 761-773
    • Slijper, M.1    Bonvin, A.M.J.J.2    Boelens, R.3    Kaptein, R.4
  • 67
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R.S., and Record, M.T., Jr. 1994. Coupling of local folding to site-specific binding of proteins to DNA. Science (Washington, D.C.), 263: 777-784.
    • (1994) Science (Washington, D.C.) , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record M.T., Jr.2
  • 68
    • 0030974118 scopus 로고    scopus 로고
    • Dual role of the NFAT insert region in DNA recognition and cooperative contact to AP-1
    • Sun, L.J., Peterson, B.R., and Verdine, G.L. 1997. Dual role of the NFAT insert region in DNA recognition and cooperative contact to AP-1. Proc. Natl. Acad. Sci. U.S.A. 94: 4919-4924.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 4919-4924
    • Sun, L.J.1    Peterson, B.R.2    Verdine, G.L.3
  • 69
    • 0026040885 scopus 로고
    • Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1: Residues that contact DNA and that transactivate
    • Thukral, S.K., Morrison, M.L., and Young, E.T. 1991. Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1: residues that contact DNA and that transactivate. Proc. Natl. Acad. Sci. U.S.A. 88: 9188-9192.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9188-9192
    • Thukral, S.K.1    Morrison, M.L.2    Young, E.T.3
  • 70
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra, N., and Bax, A. 1997. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science (Washington, D.C.), 278: 1111-1114.
    • (1997) Science (Washington, D.C.) , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 71
    • 0030963093 scopus 로고    scopus 로고
    • Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy
    • Tjandra, N., Garrett, D.S., Gronenborn, A.M., Bax, A., and Clore, G.M. 1997a. Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat. Struct. Biol. 4: 443-449.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 443-449
    • Tjandra, N.1    Garrett, D.S.2    Gronenborn, A.M.3    Bax, A.4    Clore, G.M.5
  • 74
    • 0027522642 scopus 로고
    • The acidic activation domains of the GCN4 and GAL4 proteins are not α helical but form β sheets
    • Van Hoy, M., Leuther, K.K., Kodadek, T., and Johnston, S.A. 1993. The acidic activation domains of the GCN4 and GAL4 proteins are not α helical but form β sheets. Cell, 72: 587-594.
    • (1993) Cell , vol.72 , pp. 587-594
    • Van Hoy, M.1    Leuther, K.K.2    Kodadek, T.3    Johnston, S.A.4
  • 75
    • 0029075461 scopus 로고
    • Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
    • Werner, M.H., Huth, J.R., Gronenborn, A.M., and Clore, G.M. 1995. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell, 81: 705-714.
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 78
    • 0029160486 scopus 로고
    • High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA
    • Wilson, D.S., Guenther, B., Desplan, C., and Kuriyan, J. 1995. High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA. Cell, 82: 709-719.
    • (1995) Cell , vol.82 , pp. 709-719
    • Wilson, D.S.1    Guenther, B.2    Desplan, C.3    Kuriyan, J.4
  • 79
    • 0026002757 scopus 로고
    • Crystal structure of a MATα.2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions
    • Wolberger, C., Vershon, A.K., Liu, B., Johnson, A.D., and Pabo, C.O. 1991. Crystal structure of a MATα.2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. Cell, 67: 517-528.
    • (1991) Cell , vol.67 , pp. 517-528
    • Wolberger, C.1    Vershon, A.K.2    Liu, B.3    Johnson, A.D.4    Pabo, C.O.5
  • 81
    • 0027815738 scopus 로고
    • Hydration of biological macromolecules in solution: Surface structure and molecular recognition
    • Wüthrich, K. 1993. Hydration of biological macromolecules in solution: surface structure and molecular recognition. Cold Spring Harbor Symp. Quant. Biol. 58: 149-157.
    • (1993) Cold Spring Harbor Symp. Quant. Biol. , vol.58 , pp. 149-157
    • Wüthrich, K.1
  • 83
    • 0027528411 scopus 로고
    • Refined solution structures of the Escherichia coli trp holo-and aporepressor
    • Zhao, D., Arrowsmith, C.H., Jia, X., and Jardetzky, O. 1993. Refined solution structures of the Escherichia coli trp holo-and aporepressor. J. Mol. Biol. 229: 735-746.
    • (1993) J. Mol. Biol. , vol.229 , pp. 735-746
    • Zhao, D.1    Arrowsmith, C.H.2    Jia, X.3    Jardetzky, O.4
  • 84
    • 0032489431 scopus 로고    scopus 로고
    • Solution structure of the core NFATC1/DNA complex
    • Zhou, P., Sun, L.J., Dötsch, V., Wagner, G., and Verdine, G.L. 1998. Solution structure of the core NFATC1/DNA complex. Cell, 92: 687-696.
    • (1998) Cell , vol.92 , pp. 687-696
    • Zhou, P.1    Sun, L.J.2    Dötsch, V.3    Wagner, G.4    Verdine, G.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.