메뉴 건너뛰기




Volumn 337, Issue 3, 2004, Pages 521-534

Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of c-Myb

Author keywords

CBP, CREB binding protein; Constitutive activation; CREB binding protein; HSQC, heteronuclear single quantum coherence; KID, kinase inducible activation domain; LXXLL motif; pKID, phosphorylated KID; Transcriptional activation

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; HISTIDINE; PHOSPHATE; PHOSPHOTRANSFERASE; PROTEIN C MYB; TRANSCRIPTION FACTOR;

EID: 1542358794     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.01.038     Document Type: Article
Times cited : (164)

References (48)
  • 1
    • 0034234237 scopus 로고    scopus 로고
    • CBP/p300 in cell growth, transformation, and development
    • Goodman R.H., Smolik S. CBP/p300 in cell growth, transformation, and development. Genes Dev. 14:2000;1553-1577.
    • (2000) Genes Dev. , vol.14 , pp. 1553-1577
    • Goodman, R.H.1    Smolik, S.2
  • 2
    • 0032829090 scopus 로고    scopus 로고
    • P300 and CBP: Partners for life and death
    • Giordano A., Avantaggiati M.L. p300 and CBP: partners for life and death. J. Cell. Phys. 181:1999;218-230.
    • (1999) J. Cell. Phys. , vol.181 , pp. 218-230
    • Giordano, A.1    Avantaggiati, M.L.2
  • 4
    • 0030058682 scopus 로고    scopus 로고
    • Phosphorylation of CREB at Ser133 induces complex formation with CPB via a direct mechanism
    • Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C., et al. Phosphorylation of CREB at Ser133 induces complex formation with CPB via a direct mechanism. Mol. Cell. Biol. 16:1996;694-703.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 694-703
    • Parker, D.1    Ferreri, K.2    Nakajima, T.3    Lamorte, V.J.4    Evans, R.5    Koerber, S.C.6
  • 5
    • 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., Pérez-Alvarado G.C., Parker D., Dyson H.J., Montminy M.R., Wright P.E. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell. 91:1997;741-752.
    • (1997) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Pérez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 6
    • 0036829096 scopus 로고    scopus 로고
    • Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators
    • Zor T., Mayr B.M., Dyson H.J., Montminy M.R., Wright P.E. Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators. J. Biol. Chem. 277:2002;42241-42248.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42241-42248
    • Zor, T.1    Mayr, B.M.2    Dyson, H.J.3    Montminy, M.R.4    Wright, P.E.5
  • 7
    • 0032797948 scopus 로고    scopus 로고
    • Role of secondary structure in discrimination between constitutive and inducible activators
    • Parker D., Rivera M., Zor T., Henrion-Caude A., Radhakrishnan I., Kumar A., et al. Role of secondary structure in discrimination between constitutive and inducible activators. Mol. Cell. Biol. 19:1999;5601-5607.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5601-5607
    • Parker, D.1    Rivera, M.2    Zor, T.3    Henrion-Caude, A.4    Radhakrishnan, I.5    Kumar, A.6
  • 8
    • 0031888616 scopus 로고    scopus 로고
    • Myb proteins in life, death and differentiation
    • Weston K. Myb proteins in life, death and differentiation. Curr. Opin. Genet. Dev. 8:1998;76-81.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 76-81
    • Weston, K.1
  • 9
    • 0033551402 scopus 로고    scopus 로고
    • The myb gene family in cell growth, differentiation and apoptosis
    • Oh I.H., Reddy E.P. The myb gene family in cell growth, differentiation and apoptosis. Oncogene. 18:1999;3017-3033.
    • (1999) Oncogene , vol.18 , pp. 3017-3033
    • Oh, I.H.1    Reddy, E.P.2
  • 11
    • 0344527798 scopus 로고    scopus 로고
    • Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: Implications for mapping the boundaries of structural domains
    • Radhakrishnan I., Pérez-Alvarado G.C., Parker D., Dyson H.J., Montminy M.R., Wright P.E. Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: implications for mapping the boundaries of structural domains. J. Mol. Biol. 287:1999;859-865.
    • (1999) J. Mol. Biol. , vol.287 , pp. 859-865
    • Radhakrishnan, I.1    Pérez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 12
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry
    • Baker B.M., Murphy K.P. Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biophys. J. 71:1996;2049-2055.
    • (1996) Biophys. J. , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 13
    • 0024445798 scopus 로고
    • Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine-133
    • Gonzalez G.A., Montminy M.R. Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine-133. Cell. 59:1989;675-680.
    • (1989) Cell , vol.59 , pp. 675-680
    • Gonzalez, G.A.1    Montminy, M.R.2
  • 14
    • 0034460485 scopus 로고    scopus 로고
    • Magnitude of the CREB-dependent transcriptional response is determined by the strength of the interaction between the kinase-inducible domain of CREB and the KIX domain of CREB-binding protein
    • Shaywitz A.J., Dove S.L., Kornhauser J.M., Hochschild A., Greenberg M.E. Magnitude of the CREB-dependent transcriptional response is determined by the strength of the interaction between the kinase-inducible domain of CREB and the KIX domain of CREB-binding protein. Mol. Cell. Biol. 20:2000;9409-9422.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9409-9422
    • Shaywitz, A.J.1    Dove, S.L.2    Kornhauser, J.M.3    Hochschild, A.4    Greenberg, M.E.5
  • 16
    • 0032505096 scopus 로고    scopus 로고
    • Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma
    • Nolte R.T., Wisely G.B., Westin S., Cobb J.E., Lambert M.H., Kurokawa R., et al. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 395:1998;137-143.
    • (1998) Nature , vol.395 , pp. 137-143
    • Nolte, R.T.1    Wisely, G.B.2    Westin, S.3    Cobb, J.E.4    Lambert, M.H.5    Kurokawa, R.6
  • 17
    • 0032213938 scopus 로고    scopus 로고
    • Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation
    • McInerney E.M., Rose D.W., Flynn S.E., Westin S., Mullen T.M., Krones A., et al. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev. 12:1998;3357-3368.
    • (1998) Genes Dev. , vol.12 , pp. 3357-3368
    • McInerney, E.M.1    Rose, D.W.2    Flynn, S.E.3    Westin, S.4    Mullen, T.M.5    Krones, A.6
  • 18
    • 0037203771 scopus 로고    scopus 로고
    • Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
    • Demarest S.J., Martinez-Yamout M., Chung J., Chen H., Xu W., Dyson H.J., et al. Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Nature. 415:2002;549-553.
    • (2002) Nature , vol.415 , pp. 549-553
    • Demarest, S.J.1    Martinez-Yamout, M.2    Chung, J.3    Chen, H.4    Xu, W.5    Dyson, H.J.6
  • 19
    • 0032982862 scopus 로고    scopus 로고
    • Electrostatic contribution of phosphorylation to the stability of the CREB-CBP activator-coactivator complex
    • Mestas S.P., Lumb K.J. Electrostatic contribution of phosphorylation to the stability of the CREB-CBP activator-coactivator complex. Nature Struct. Biol. 6:1999;613-614.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 613-614
    • Mestas, S.P.1    Lumb, K.J.2
  • 20
    • 0031014535 scopus 로고    scopus 로고
    • Oncogenic activation of c-Myb by carboxyl-terminal truncation leads to decreased proteolysis by the ubiquitin-26S proteasome pathway
    • Bies J., Wolff L. Oncogenic activation of c-Myb by carboxyl-terminal truncation leads to decreased proteolysis by the ubiquitin-26S proteasome pathway. Oncogene. 14:1997;203-212.
    • (1997) Oncogene , vol.14 , pp. 203-212
    • Bies, J.1    Wolff, L.2
  • 22
    • 0021234035 scopus 로고
    • Expression of myb, myc and fos proto-oncogenes during the differentiation of a murine myeloid leukaemia
    • Gonda T.J., Metcalf D. Expression of myb, myc and fos proto-oncogenes during the differentiation of a murine myeloid leukaemia. Nature. 310:1984;249-251.
    • (1984) Nature , vol.310 , pp. 249-251
    • Gonda, T.J.1    Metcalf, D.2
  • 23
    • 0027166104 scopus 로고
    • Coupling of hormonal stimulation and transcription via the cyclic AMP-responsive factor CREB is rate limited by nuclear entry of protein kinase a
    • Hagiwara M., Brindle P., Harootunian A., Armstrong R., Rivier J., Vale W., et al. Coupling of hormonal stimulation and transcription via the cyclic AMP-responsive factor CREB is rate limited by nuclear entry of protein kinase A. Mol. Cell. Biol. 13:1993;4852-4859.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4852-4859
    • Hagiwara, M.1    Brindle, P.2    Harootunian, A.3    Armstrong, R.4    Rivier, J.5    Vale, W.6
  • 24
    • 0026653422 scopus 로고
    • Transcriptional attenuation following cAMP induction requires PP-1-mediated dephosphorylation of CREB
    • Hagiwara M., Alberts A., Brindle P., Meinkoth J., Feramisco J., Deng T., et al. Transcriptional attenuation following cAMP induction requires PP-1-mediated dephosphorylation of CREB. Cell. 70:1992;105-113.
    • (1992) Cell , vol.70 , pp. 105-113
    • Hagiwara, M.1    Alberts, A.2    Brindle, P.3    Meinkoth, J.4    Feramisco, J.5    Deng, T.6
  • 25
    • 0034141972 scopus 로고    scopus 로고
    • CREB-binding protein and p300: Molecular integrators of hematopoietic transcription
    • Blobel G.A. CREB-binding protein and p300: molecular integrators of hematopoietic transcription. Blood. 95:2000;745-755.
    • (2000) Blood , vol.95 , pp. 745-755
    • Blobel, G.A.1
  • 26
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 proteins: Active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion G., Avruch J. 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J. Biol. Chem. 277:2002;3061-3064.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 27
    • 0031470652 scopus 로고    scopus 로고
    • The structural basis for 14-3-3: Phosphopeptide binding specificity
    • Yaffe M.B., Rittinger K., Volinia S., Caron P.R., Aitken A., Leffers H., et al. The structural basis for 14-3-3: phosphopeptide binding specificity. Cell. 91:1997;961-971.
    • (1997) Cell , vol.91 , pp. 961-971
    • Yaffe, M.B.1    Rittinger, K.2    Volinia, S.3    Caron, P.R.4    Aitken, A.5    Leffers, H.6
  • 28
    • 0033554398 scopus 로고    scopus 로고
    • Residues of 14-3-3 zeta required for activation of exoenzyme S of Pseudomonas aeruginosa
    • Zhang L., Wang H., Masters S.C., Wang B., Barbieri J.T., Fu H. Residues of 14-3-3 zeta required for activation of exoenzyme S of Pseudomonas aeruginosa. Biochemistry. 38:1999;12159-12164.
    • (1999) Biochemistry , vol.38 , pp. 12159-12164
    • Zhang, L.1    Wang, H.2    Masters, S.C.3    Wang, B.4    Barbieri, J.T.5    Fu, H.6
  • 29
    • 0033586783 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa
    • Masters S.C., Pederson K.J., Zhang L., Barbieri J.T., Fu H. Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa. Biochemistry. 38:1999;5216-5221.
    • (1999) Biochemistry , vol.38 , pp. 5216-5221
    • Masters, S.C.1    Pederson, K.J.2    Zhang, L.3    Barbieri, J.T.4    Fu, H.5
  • 30
    • 0033592326 scopus 로고    scopus 로고
    • Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display
    • Wang B., Yang H., Liu Y.C., Jelinek T., Zhang L., Ruoslahti E., Fu H. Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display. Biochemistry. 38:1999;12499-12504.
    • (1999) Biochemistry , vol.38 , pp. 12499-12504
    • Wang, B.1    Yang, H.2    Liu, Y.C.3    Jelinek, T.4    Zhang, L.5    Ruoslahti, E.6    Fu, H.7
  • 31
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3 zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa C., Masters S.C., Bankston L.A., Pohl J., Wang B.C., Fu H.I., Liddington R.C. 14-3-3 zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J. Biol. Chem. 273:1998;16305-16310.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16305-16310
    • Petosa, C.1    Masters, S.C.2    Bankston, L.A.3    Pohl, J.4    Wang, B.C.5    Fu, H.I.6    Liddington, R.C.7
  • 33
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson B.A., Blevins R.A. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:1994;604-613.
    • (1994) J. Biomol. NMR , vol.4 , pp. 604-613
    • Johnson, B.A.1    Blevins, R.A.2
  • 34
    • 44049109615 scopus 로고
    • An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins
    • Grzesiek S., Bax A. An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J. Magn. Reson. 99:1992;201-207.
    • (1992) J. Magn. Reson. , vol.99 , pp. 201-207
    • Grzesiek, S.1    Bax, A.2
  • 35
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • Wittekind M., Mueller L. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J. Magn. Reson. 101:1993;201-205.
    • (1993) J. Magn. Reson. , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 36
    • 9444245493 scopus 로고
    • Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek S., Bax A. Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114:1992;6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 37
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A., Grzesiek S. Methodological advances in protein NMR. Acc. Chem. Res. 26:1993;131-138.
    • (1993) Acc. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 38
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • Kay L.E., Ikura M., Tschudin R., Bax A. Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89:1990;496-514.
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 39
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR. 4:1994;845-858.
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 44
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart D.S., Sykes B.D. Chemical shifts as a tool for structure determination. Methods Enzymol. 239:1994;363-392.
    • (1994) Methods Enzymol. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 45
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P., Mumenthaler C., Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273:1997;283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 46
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman D.A., Case D.A., Caldwell J.W., Ross W.S., Cheatham T.E. III, DeBolt S., et al. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comp. Phys. Commun. 91:1995;1-41.
    • (1995) Comp. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham III, T.E.5    Debolt, S.6
  • 47
  • 48
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.