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Volumn 22, Issue 4, 2009, Pages 261-269

The Max homodimeric b-HLH-LZ significantly interferes with the specific heterodimerization between the c-Myc and Max b-HLH-LZ in absence of DNA: A quantitative analysis

Author keywords

B HLH LZ; C Myc; CD; Max; NMR; Specific heterodimerization; Thermodynamic simulations

Indexed keywords

BASIC HELIX LOOP HELIX LEUCINE ZIPPER TRANSCRIPTION FACTOR; DNA; MYC PROTEIN;

EID: 67650257998     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.938     Document Type: Article
Times cited : (22)

References (34)
  • 1
    • 23144464363 scopus 로고    scopus 로고
    • Transcriptional regulation and transformation by Myc proteins
    • Adhikary S., Eilers M. 2005. Transcriptional regulation and transformation by Myc proteins. Nat. Rev. Mol. Cell Biol. 6: 635-645.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 635-645
    • Adhikary, S.1    Eilers, M.2
  • 2
    • 0027533679 scopus 로고
    • Oncogenic activity of the c-Myc protein requires dimerization with Max
    • Amati B., Brooks MW, Levy N., Littlewood TD, Evan GI, Land H. 1993. Oncogenic activity of the c-Myc protein requires dimerization with Max. Cell 72: 233-245.
    • (1993) Cell , vol.72 , pp. 233-245
    • Amati, B.1    Brooks, M.W.2    Levy, N.3    Littlewood, T.D.4    Evan, G.I.5    Land, H.6
  • 3
    • 33144472690 scopus 로고    scopus 로고
    • Thermodynamics of protein-protein interactions of cMyc, Max, and Mad: Effect of polyions on protein dimerization
    • Banerjee A., Hu J., Goss DJ. 2006. Thermodynamics of protein-protein interactions of cMyc, Max, and Mad: effect of polyions on protein dimerization. Biochemistry 45: 2333-2338.
    • (2006) Biochemistry , vol.45 , pp. 2333-2338
    • Banerjee, A.1    Hu, J.2    Goss, D.J.3
  • 4
    • 0025763419 scopus 로고
    • Max: A helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc
    • Blackwood EM, Eisenman RN. 1991. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Nature 251: 1211-1217.
    • (1991) Nature , vol.251 , pp. 1211-1217
    • Blackwood, E.M.1    Eisenman, R.N.2
  • 6
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson M. 1987. Ribbon models of macromolecules. J. Mol. Graph. 5: 103-106.
    • (1987) J. Mol. Graph , vol.5 , pp. 103-106
    • Carson, M.1
  • 7
    • 0034495086 scopus 로고    scopus 로고
    • Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR
    • Cave JW, Kremer W., Wemmer DE. 2000. Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR. Protein Sci. 91: 2354-2365.
    • (2000) Protein Sci , vol.91 , pp. 2354-2365
    • Cave, J.W.1    Kremer, W.2    Wemmer, D.E.3
  • 8
    • 0037067653 scopus 로고    scopus 로고
    • E2F4/5 and p107 as Smad cofactors linking the TGF-β receptor to c-myc repression
    • Chen CR, Kang Y., Siegel M., Massagué J. 2002. E2F4/5 and p107 as Smad cofactors linking the TGF-β receptor to c-myc repression. Genes Dev. 110: 19-32.
    • (2002) Genes Dev , vol.110 , pp. 19-32
    • Chen, C.R.1    Kang, Y.2    Siegel, M.3    Massagué, J.4
  • 9
    • 0031933143 scopus 로고    scopus 로고
    • Determining structures of large proteins and protein complexes by NMR
    • Clore GM, Gronenborn AM. 1998. Determining structures of large proteins and protein complexes by NMR. Trends Biotechnol. 16: 22-34.
    • (1998) Trends Biotechnol , vol.16 , pp. 22-34
    • Clore, G.M.1    Gronenborn, A.M.2
  • 12
    • 67650232999 scopus 로고    scopus 로고
    • DeLano Scientific LLC, San Carlos, CA, USA
    • DeLano WL. 2002. The PyMOL Molecular Graphics System. DeLano Scientific LLC, San Carlos, CA, USA. http://www.pymol.org
    • (2002)
    • DeLano, W.L.1
  • 13
    • 0027910469 scopus 로고
    • Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
    • Ferré-D'Amaré AR, Prendergast GC, Ziff EB, Burley SK. 1993. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 363: 38-45.
    • (1993) Nature , vol.363 , pp. 38-45
    • Ferré-D'Amaré, A.R.1    Prendergast, G.C.2    Ziff, E.B.3    Burley, S.K.4
  • 14
    • 0035853279 scopus 로고    scopus 로고
    • Structure, function, and dynamics of the dimerization and DNA- binding domain of oncogenic transcription factor v-Myc
    • Fieber W., Schneider ML, Matt T., Krautler B., Konrat R., Bister K. 2001. Structure, function, and dynamics of the dimerization and DNA- binding domain of oncogenic transcription factor v-Myc. J. Mol. Biol. 307: 1395-1410.
    • (2001) J. Mol. Biol , vol.307 , pp. 1395-1410
    • Fieber, W.1    Schneider, M.L.2    Matt, T.3    Krautler, B.4    Konrat, R.5    Bister, K.6
  • 16
    • 0027536102 scopus 로고
    • Opposite regulation of gene transcription and cell proliferation by c-Myc and Max
    • Gu W., Cechova K., Tassi V., Dalla-Favera R. 1993. Opposite regulation of gene transcription and cell proliferation by c-Myc and Max. Proc. Natl Acad. Sci. USA 90: 2935-2939.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2935-2939
    • Gu, W.1    Cechova, K.2    Tassi, V.3    Dalla-Favera, R.4
  • 17
    • 0029686266 scopus 로고    scopus 로고
    • Proteins of the Myc network: Essential regulators of cell growth and differentiation
    • Henriksson M., Lüsher B. 1996. Proteins of the Myc network: essential regulators of cell growth and differentiation. Advan. Cancer Res. 68: 109-182.
    • (1996) Advan. Cancer Res , vol.68 , pp. 109-182
    • Henriksson, M.1    Lüsher, B.2
  • 19
    • 34249765651 scopus 로고
    • NMRview: A computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA. 1994. NMRview: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4: 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 20
    • 0028800087 scopus 로고
    • Field gradient techniques in NMR spectroscopy
    • Kay LE. 1995. Field gradient techniques in NMR spectroscopy. Curr. Opin. Struct. Biol. 5: 674-681.
    • (1995) Curr. Opin. Struct. Biol , vol.5 , pp. 674-681
    • Kay, L.E.1
  • 22
    • 0026737875 scopus 로고
    • Myc and Max proteins possess distinct transcriptional activities
    • Kretzner L., Blackwood EM, Eisenman RN. 1992. Myc and Max proteins possess distinct transcriptional activities. Nature 359: 426-429.
    • (1992) Nature , vol.359 , pp. 426-429
    • Kretzner, L.1    Blackwood, E.M.2    Eisenman, R.N.3
  • 25
    • 0029563395 scopus 로고
    • Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc Leucine zippers: A description of putative electrostatic interactions responsible for the specificity of heterodimerization
    • Lavigne P., Kondejewski LH, Houston ME Jr, Sönnichsen FD, Lix B., Sykes BD, Hodges RS, Kay CM. 1995. Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc Leucine zippers: a description of putative electrostatic interactions responsible for the specificity of heterodimerization. J. Mol. Biol. 254: 505-520.
    • (1995) J. Mol. Biol , vol.254 , pp. 505-520
    • Lavigne, P.1    Kondejewski, L.H.2    Houston Jr, M.E.3    Sönnichsen, F.D.4    Lix, B.5    Sykes, B.D.6    Hodges, R.S.7    Kay, C.M.8
  • 27
    • 38049000375 scopus 로고    scopus 로고
    • Elucidation of the structural determinants responsible for the specific formation of heterodimeric Mxd1/Max b-HLH-LZ and its binding to E-box sequences
    • Montagne M., Naud J-F, Lavigne P. 2008. Elucidation of the structural determinants responsible for the specific formation of heterodimeric Mxd1/Max b-HLH-LZ and its binding to E-box sequences. J. Mol. Biol. 376: 141-152.
    • (2008) J. Mol. Biol , vol.376 , pp. 141-152
    • Montagne, M.1    Naud, J.-F.2    Lavigne, P.3
  • 28
    • 0028839440 scopus 로고
    • The leucine zippers of the HLH-LZ proteins Max and c-Myc preferentially form heterodimers
    • Muhle-Goll C., Nilges M., Pastore A. 1995. The leucine zippers of the HLH-LZ proteins Max and c-Myc preferentially form heterodimers. Biochemistry 34: 13554-13564.
    • (1995) Biochemistry , vol.34 , pp. 13554-13564
    • Muhle-Goll, C.1    Nilges, M.2    Pastore, A.3
  • 29
    • 0037462459 scopus 로고    scopus 로고
    • X-ray structures of Myc-Max and Mad-Max recognizing DNA: Molecular bases of regulation by proto-oncogenic transcription factors
    • Nair SK, Burley SK. 2003. X-ray structures of Myc-Max and Mad-Max recognizing DNA: molecular bases of regulation by proto-oncogenic transcription factors. Cell 112: 193-205.
    • (2003) Cell , vol.112 , pp. 193-205
    • Nair, S.K.1    Burley, S.K.2
  • 30
    • 0037424651 scopus 로고    scopus 로고
    • Improving the Stability of the LZ domain of Max increases the stability of its B-HLH-LZ:E-Box complex
    • Naud J-F, Gagnon F., Wellinger R., Chabot B., Lavigne P. 2003. Improving the Stability of the LZ domain of Max increases the stability of its B-HLH-LZ:E-Box complex. J. Mol. Biol. 326: 1577-1595.
    • (2003) J. Mol. Biol , vol.326 , pp. 1577-1595
    • Naud, J.-F.1    Gagnon, F.2    Wellinger, R.3    Chabot, B.4    Lavigne, P.5
  • 32
    • 4444234733 scopus 로고    scopus 로고
    • The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: Insights into the specific and reversible DNA binding mechanism of dimeric transcription factors
    • Sauvé S., Tremblay L., Lavigne P. 2004. The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors. J. Mol. Biol. 342: 813-832.
    • (2004) J. Mol. Biol , vol.342 , pp. 813-832
    • Sauvé, S.1    Tremblay, L.2    Lavigne, P.3
  • 33
    • 0024384644 scopus 로고
    • Preferential heterodimer formation by isolated leucine zippers from fos and jun
    • O'Shea EK, Rutkowski R., Stafford WF 3rd, Kim PS. 1989. Preferential heterodimer formation by isolated leucine zippers from fos and jun. Science 24: 646-648.
    • (1989) Science , vol.24 , pp. 646-648
    • O'Shea, E.K.1    Rutkowski, R.2    Stafford 3rd, W.F.3    Kim, P.S.4
  • 34
    • 0029364052 scopus 로고    scopus 로고
    • Wishart DS, Bigam CG, Yao J., AbildgaardF, Dyson HJ, Oldfield E., Markley JL, Sykes BD. 1995. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6: 135-140.
    • Wishart DS, Bigam CG, Yao J., AbildgaardF, Dyson HJ, Oldfield E., Markley JL, Sykes BD. 1995. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6: 135-140.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.