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Volumn 427, Issue 2, 2010, Pages 225-236

Mutants of the tumour suppressor p53 L1 loop as second-site suppressors for restoring DNA binding to oncogenic p53 mutations: Structural and biochemical insights

Author keywords

Cancer; DNA binding; Molecular dynamics simulation (MD simulation); p53 mutant; Protein folding; Thermal stability

Indexed keywords

DNA BINDING; MD SIMULATION; MOLECULAR DYNAMICS SIMULATIONS; P53 MUTANTS; THERMAL STABILITY;

EID: 77952755475     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20091888     Document Type: Article
Times cited : (25)

References (55)
  • 1
    • 58149199126 scopus 로고    scopus 로고
    • Structural and functional basis for therapeutic modulation of p53 signaling
    • Bassett, E. A., Wang, W., Rastinejad, F. and El-Deiry, W. S. (2008) Structural and functional basis for therapeutic modulation of p53 signaling. Clin. Cancer Res. 14, 6376-6386
    • (2008) Clin. Cancer Res. , vol.14 , pp. 6376-6386
    • Bassett, E.A.1    Wang, W.2    Rastinejad, F.3    El-Deiry, W.S.4
  • 2
    • 0034668786 scopus 로고    scopus 로고
    • Strategies for manipulating the p53 pathway in the treatment of human cancer
    • Hupp, T. R., Lane, D. P. and Ball, K. L. (2000) Strategies for manipulating the p53 pathway in the treatment of human cancer. Biochem. J. 352, 1-17
    • (2000) Biochem. J. , vol.352 , pp. 1-17
    • Hupp, T.R.1    Lane, D.P.2    Ball, K.L.3
  • 5
    • 34047224955 scopus 로고    scopus 로고
    • Structure-function-rescue: The diverse nature of common p53 cancer mutants
    • Joerger, A. C. and Fersht, A. R. (2007) Structure-function-rescue: the diverse nature of common p53 cancer mutants. Oncogene 26, 2226-2242
    • (2007) Oncogene , vol.26 , pp. 2226-2242
    • Joerger, A.C.1    Fersht, A.R.2
  • 6
    • 47649096991 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53
    • Joerger, A. C. and Fersht, A. R. (2008) Structural biology of the tumor suppressor p53. Annu. Rev. Biochem. 77, 557-582
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 557-582
    • Joerger, A.C.1    Fersht, A.R.2
  • 7
    • 34047209861 scopus 로고    scopus 로고
    • Reactivation of mutant p53: Molecular mechanisms and therapeutic potential
    • Selivanova, G. and Wiman, K. G. (2007) Reactivation of mutant p53: molecular mechanisms and therapeutic potential. Oncogene 26, 2243-2254
    • (2007) Oncogene , vol.26 , pp. 2243-2254
    • Selivanova, G.1    Wiman, K.G.2
  • 9
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho, Y., Gorina, S., Jeffrey, P. D. and Pavletich, N. P. (1994) Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265, 346-355
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 10
    • 34047174813 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53 and cancer-associated mutants
    • Joerger, A. C. and Fersht, A. R. (2007) Structural biology of the tumor suppressor p53 and cancer-associated mutants. Adv. Cancer Res. 97, 1-23
    • (2007) Adv. Cancer Res. , vol.97 , pp. 1-23
    • Joerger, A.C.1    Fersht, A.R.2
  • 12
    • 0032055501 scopus 로고    scopus 로고
    • Genetic selection of intragenic suppressor mutations that reverse the effect of common p53 cancer mutations
    • Brachmann, R. K., Yu, K., Eby, Y., Pavletich, N. P. and Boeke, J. D. (1998) Genetic selection of intragenic suppressor mutations that reverse the effect of common p53 cancer mutations. EMBO J. 17, 1847-1859
    • (1998) EMBO J. , vol.17 , pp. 1847-1859
    • Brachmann, R.K.1    Yu, K.2    Eby, Y.3    Pavletich, N.P.4    Boeke, J.D.5
  • 16
    • 0032437592 scopus 로고    scopus 로고
    • Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability
    • Nikolova, P. V., Henckel, J., Lane, D. P. and Fersht, A. R. (1998) Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability. Proc. Natl. Acad. Sci. U.S.A. 95, 14675-14680
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14675-14680
    • Nikolova, P.V.1    Henckel, J.2    Lane, D.P.3    Fersht, A.R.4
  • 17
    • 0034141471 scopus 로고    scopus 로고
    • Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations
    • Nikolova, P. V., Wong, K. B., DeDecker, B., Henckel, J. and Fersht, A. R. (2000) Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations. EMBO J. 19, 370-378 (Pubitemid 30072607)
    • (2000) EMBO Journal , vol.19 , Issue.3 , pp. 370-378
    • Nikolova, P.V.1    Wong, K.-B.2    Dedecker, B.3    Henckel, J.4    Fersht, A.R.5
  • 18
    • 33746790624 scopus 로고    scopus 로고
    • Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains
    • Ang, H. C., Joerger, A. C., Mayer, S. and Fersht, A. R. (2006) Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains. J. Biol. Chem. 281, 21934-21941
    • (2006) J. Biol. Chem. , vol.281 , pp. 21934-21941
    • Ang, H.C.1    Joerger, A.C.2    Mayer, S.3    Fersht, A.R.4
  • 19
    • 13444267551 scopus 로고    scopus 로고
    • In the quest for stable rescuing mutants of p53: Computational mutagenesis of flexible loop L1
    • Pan, Y., Ma, B., Venkataraghavan, R. B., Levine, A. J. and Nussinov, R. (2005) In the quest for stable rescuing mutants of p53: computational mutagenesis of flexible loop L1. Biochemistry 44, 1423-1432
    • (2005) Biochemistry , vol.44 , pp. 1423-1432
    • Pan, Y.1    Ma, B.2    Venkataraghavan, R.B.3    Levine, A.J.4    Nussinov, R.5
  • 20
    • 49149090309 scopus 로고    scopus 로고
    • p53-induced DNA bending: The interplay between p53-DNA and p53-p53 interactions
    • Pan, Y. and Nussinov, R. (2008) p53-induced DNA bending: the interplay between p53-DNA and p53-p53 interactions. J. Phys. Chem. B 112, 6716-6724
    • (2008) J. Phys. Chem. B , vol.112 , pp. 6716-6724
    • Pan, Y.1    Nussinov, R.2
  • 22
    • 0035821734 scopus 로고    scopus 로고
    • Novel human p53 mutations that are toxic to yeast can enhance transactivation of specific promoters and reactivate tumor p53 mutants
    • Inga, A. and Resnick, M. A. (2001) Novel human p53 mutations that are toxic to yeast can enhance transactivation of specific promoters and reactivate tumor p53 mutants. Oncogene 20, 3409-3419
    • (2001) Oncogene , vol.20 , pp. 3409-3419
    • Inga, A.1    Resnick, M.A.2
  • 23
    • 33746012703 scopus 로고    scopus 로고
    • Mutational analysis of the p53 core domain L1 loop
    • Zupnick, A. and Prives, C. (2006) Mutational analysis of the p53 core domain L1 loop. J. Biol. Chem. 281, 20464-20473
    • (2006) J. Biol. Chem. , vol.281 , pp. 20464-20473
    • Zupnick, A.1    Prives, C.2
  • 24
    • 0035853734 scopus 로고    scopus 로고
    • Crystal structure of the mouse p53 core DNA-binding domain at 2.7 Å resolution
    • Zhao, K., Chai, X., Johnston, K., Clements, A. and Marmorstein, R. (2001) Crystal structure of the mouse p53 core DNA-binding domain at 2.7 Å resolution. J. Biol. Chem. 276, 12120-12127
    • (2001) J. Biol. Chem. , vol.276 , pp. 12120-12127
    • Zhao, K.1    Chai, X.2    Johnston, K.3    Clements, A.4    Marmorstein, R.5
  • 25
    • 0347723910 scopus 로고    scopus 로고
    • Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations
    • Joerger, A. C., Allen, M. D. and Fersht, A. R. (2004) Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations. J. Biol. Chem. 279, 1291-1296
    • (2004) J. Biol. Chem. , vol.279 , pp. 1291-1296
    • Joerger, A.C.1    Allen, M.D.2    Fersht, A.R.3
  • 26
    • 33750036093 scopus 로고    scopus 로고
    • Structural basis for understanding oncogenic p53 mutations and designing rescue drugs
    • Joerger, A. C., Ang, H. C. and Fersht, A. R. (2006) Structural basis for understanding oncogenic p53 mutations and designing rescue drugs. Proc. Natl. Acad. Sci. U.S.A. 103, 15056-15061
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 15056-15061
    • Joerger, A.C.1    Ang, H.C.2    Fersht, A.R.3
  • 27
    • 18144387188 scopus 로고    scopus 로고
    • Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations
    • Joerger, A. C., Ang, H. C., Veprintsev, D. B., Blair, C. M. and Fersht, A. R. (2005) Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations. J. Biol. Chem. 280, 16030-16037
    • (2005) J. Biol. Chem. , vol.280 , pp. 16030-16037
    • Joerger, A.C.1    Ang, H.C.2    Veprintsev, D.B.3    Blair, C.M.4    Fersht, A.R.5
  • 29
    • 33746002633 scopus 로고    scopus 로고
    • Structure of the p53 core domain dimer bound to DNA
    • Ho, W. C., Fitzgerald, M. X. and Marmorstein, R. (2006) Structure of the p53 core domain dimer bound to DNA. J. Biol. Chem. 281, 20494-20502
    • (2006) J. Biol. Chem. , vol.281 , pp. 20494-20502
    • Ho, W.C.1    Fitzgerald, M.X.2    Marmorstein, R.3
  • 31
    • 33645456248 scopus 로고    scopus 로고
    • Comparison of the human and worm p53 structures suggests a way for enhancing stability
    • Pan, Y., Ma, B., Levine, A. J. and Nussinov, R. (2006) Comparison of the human and worm p53 structures suggests a way for enhancing stability. Biochemistry 45, 3925-3933
    • (2006) Biochemistry , vol.45 , pp. 3925-3933
    • Pan, Y.1    Ma, B.2    Levine, A.J.3    Nussinov, R.4
  • 32
    • 0035945659 scopus 로고    scopus 로고
    • P53 mutants exhibiting enhanced transcriptional activation and altered promoter selectivity are revealed using a sensitive, yeast-based functional assay
    • DOI 10.1038/sj.onc.1204116
    • Inga, A., Monti, P., Fronza, G., Darden, T. and Resnick, M. A. (2001) p53 mutants exhibiting enhanced transcriptional activation and altered promoter selectivity are revealed using a sensitive, yeast-based functional assay. Oncogene 20, 501-513 (Pubitemid 32158230)
    • (2001) Oncogene , vol.20 , Issue.4 , pp. 501-513
    • Inga, A.1    Monti, P.2    Fronza, G.3    Darden, T.4    Resnick, M.A.5
  • 34
    • 34547661589 scopus 로고    scopus 로고
    • Directed evolution of p53 variants with altered DNA-binding specificities by in vitro compartmentalization
    • Fen, C. X., Coomber, D. W., Lane, D. P. and Ghadessy, F. J. (2007) Directed evolution of p53 variants with altered DNA-binding specificities by in vitro compartmentalization. J. Mol. Biol. 371, 1238-1248
    • (2007) J. Mol. Biol. , vol.371 , pp. 1238-1248
    • Fen, C.X.1    Coomber, D.W.2    Lane, D.P.3    Ghadessy, F.J.4
  • 36
    • 34250800246 scopus 로고    scopus 로고
    • The screening of the second-site suppressor mutations of the common p53 mutants
    • Otsuka, K., Kato, S., Kakudo, Y., Mashiko, S., Shibata, H. and Ishioka, C. (2007) The screening of the second-site suppressor mutations of the common p53 mutants. Int. J. Cancer 121, 559-566
    • (2007) Int. J. Cancer , vol.121 , pp. 559-566
    • Otsuka, K.1    Kato, S.2    Kakudo, Y.3    Mashiko, S.4    Shibata, H.5    Ishioka, C.6
  • 37
    • 0347130901 scopus 로고    scopus 로고
    • Structural distortion of p53 by the mutation R249S and its rescue by a designed peptide: Implications for mutant conformation
    • Friedler, A., DeDecker, B. S., Freund, S. M., Blair, C., Rudiger, S. and Fersht, A. R. (2004) Structural distortion of p53 by the mutation R249S and its rescue by a designed peptide: implications for 'mutant conformation'. J. Mol. Biol. 336, 187-196
    • (2004) J. Mol. Biol. , vol.336 , pp. 187-196
    • Friedler, A.1    DeDecker, B.S.2    Freund, S.M.3    Blair, C.4    Rudiger, S.5    Fersht, A.R.6
  • 38
    • 40549119464 scopus 로고    scopus 로고
    • The p73 DNA binding domain displays enhanced stability relative to its homologue, the tumor suppressor p53, and exhibits cooperative DNA binding
    • Patel, S., Bui, T. T. T., Drake, A. F., Fraternali, F. and Nikolova, P. V. (2008) The p73 DNA binding domain displays enhanced stability relative to its homologue, the tumor suppressor p53, and exhibits cooperative DNA binding. Biochemistry 47, 3235-3244
    • (2008) Biochemistry , vol.47 , pp. 3235-3244
    • Patel, S.1    Bui, T.T.T.2    Drake, A.F.3    Fraternali, F.4    Nikolova, P.V.5
  • 39
    • 52649151797 scopus 로고    scopus 로고
    • Molecular interactions of ASPP1 and ASPP2 with the p53 protein family and the apoptotic promoters PUMA and Bax
    • Patel, S., George, R., Autore, F., Fraternali, F., Ladbury, J. E. and Nikolova, P. V. (2008) Molecular interactions of ASPP1 and ASPP2 with the p53 protein family and the apoptotic promoters PUMA and Bax. Nucleic Acids Res. 36, 5139-5151
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5139-5151
    • Patel, S.1    George, R.2    Autore, F.3    Fraternali, F.4    Ladbury, J.E.5    Nikolova, P.V.6
  • 40
    • 77954932038 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 42
    • 46249092554 scopus 로고    scopus 로고
    • Gromacs 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., van Der Spoel, D. and Lindahl, E. (2008) Gromacs 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 43
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink, C., Villa, A., Mark, A. E. and van Gunsteren, W. F. (2004) A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6. J. Comput. Chem. 25, 1656-1676
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 44
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • Pullman, B., ed., D. Reidel, Dordrecht
    • Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F. and Hermans, J. (1981) Interaction models for water in relation to protein hydration. In Intermolecular Forces (Pullman, B., ed.), pp. 331-342, D. Reidel, Dordrecht
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 45
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulation
    • Hess, B., Bekker, H., Berendsen, H. J. C. and Fraaije, J. (1997) LINCS: a linear constraint solver for molecular simulation. J. Comput. Chem. 18, 1463-1472
    • (1997) J. Comput. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.4
  • 47
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G., Donadiao, D. and Parrinello, M. (2007) Canonical sampling through velocity rescaling. J. Chem. Phys. 126, 014101
    • (2007) J. Chem. Phys. , vol.126 , pp. 014101
    • Bussi, G.1    Donadiao, D.2    Parrinello, M.3
  • 51
    • 0037591875 scopus 로고    scopus 로고
    • Kinetic instability of p53 core domain mutants: Implications for rescue by small molecules
    • Friedler, A., Veprintsev, D. B., Hansson, L. O. and Fersht, A. R. (2003) Kinetic instability of p53 core domain mutants: implications for rescue by small molecules. J. Biol. Chem. 278, 24108-24112
    • (2003) J. Biol. Chem. , vol.278 , pp. 24108-24112
    • Friedler, A.1    Veprintsev, D.B.2    Hansson, L.O.3    Fersht, A.R.4
  • 53
    • 34547687667 scopus 로고    scopus 로고
    • Correlation of levels of folded recombinant p53 in Escherichia coliwith thermodynamic stability in vitro
    • Mayer, S., Rudiger, S., Ang, H. C., Joerger, A. C. and Fersht, A. R. (2007) Correlation of levels of folded recombinant p53 in Escherichia coliwith thermodynamic stability in vitro. J. Mol. Biol. 372, 268-276
    • (2007) J. Mol. Biol. , vol.372 , pp. 268-276
    • Mayer, S.1    Rudiger, S.2    Ang, H.C.3    Joerger, A.C.4    Fersht, A.R.5
  • 54
    • 35348950535 scopus 로고    scopus 로고
    • Molecular dynamics simulations of p53 DNA-binding domain
    • Lu, Q., Tan, Y.-H. and Luo, R. (2007) Molecular dynamics simulations of p53 DNA-binding domain. J. Phys. Chem. B 111, 11538-11545
    • (2007) J. Phys. Chem. B , vol.111 , pp. 11538-11545
    • Lu, Q.1    Tan, Y.-H.2    Luo, R.3
  • 55
    • 41949120867 scopus 로고    scopus 로고
    • Stability of the core domain of p53: Insights from computer simulations
    • Madhumalar, A., Smith, D. J. and Verma, C. (2008) Stability of the core domain of p53: insights from computer simulations. BMC Bioinformatics 9, 1-15
    • (2008) BMC Bioinformatics , vol.9 , pp. 1-15
    • Madhumalar, A.1    Smith, D.J.2    Verma, C.3


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