메뉴 건너뛰기




Volumn 12, Issue 1, 2011, Pages 128-140

Insight into a novel p53 single point mutation (G389E) by molecular dynamics simulations

Author keywords

Molecular dynamics; P53; Protein interactions; S100B

Indexed keywords

GLUTAMIC ACID; GLYCINE; MUTANT PROTEIN; PROTEIN P53; PROTEIN S100B;

EID: 79251630875     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12010128     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H.; Wright, P. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 2002, 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.1    Wright, P.2
  • 3
    • 0034676455 scopus 로고    scopus 로고
    • Surfing the p53 network
    • Vogelstein, B.; Lane, D.; Levine, A. Surfing the p53 network. Nature 2000, 408, 307-310.
    • (2000) Nature , vol.408 , pp. 307-310
    • Vogelstein, B.1    Lane, D.2    Levine, A.3
  • 4
    • 0032055501 scopus 로고    scopus 로고
    • Genetic selection of intragenic suppressor mutations that reverse the effect of common p53 cancer mutations
    • Brachmann, R.; Yu, K.; Eby, Y.; Pavletich, N.; Boeke, J. Genetic selection of intragenic suppressor mutations that reverse the effect of common p53 cancer mutations. EMBO J. 1998, 17, 1847-1859.
    • (1998) EMBO J , vol.17 , pp. 1847-1859
    • Brachmann, R.1    Yu, K.2    Eby, Y.3    Pavletich, N.4    Boeke, J.5
  • 5
    • 0037816165 scopus 로고    scopus 로고
    • Understanding the function-structure and function-mutation relationships of p53 tumor suppressor protein by high-resolution missense mutation analysis
    • Kato, S.; Han, S.; Liu, W.; Otsuka, K.; Shibata, H.; Kanamaru, R.; Ishioka, C. Understanding the function-structure and function-mutation relationships of p53 tumor suppressor protein by high-resolution missense mutation analysis. Proc. Natl. Acad. Sci. USA 2003, 100, 8424-8429.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8424-8429
    • Kato, S.1    Han, S.2    Liu, W.3    Otsuka, K.4    Shibata, H.5    Kanamaru, R.6    Ishioka, C.7
  • 6
    • 0034862475 scopus 로고    scopus 로고
    • The C-terminus of p53: The more you learn the less you know
    • Ahn, J.; Prives, C. The C-terminus of p53: The more you learn the less you know. Nat. Struct. Biol. 2001, 8, 730-732.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 730-732
    • Ahn, J.1    Prives, C.2
  • 7
    • 0028519273 scopus 로고
    • Allosteric activation of latent p53 tetramers
    • Hupp, T.; Lane, D. Allosteric activation of latent p53 tetramers. Curr. Biol. 1994, 4, 865-875.
    • (1994) Curr. Biol , vol.4 , pp. 865-875
    • Hupp, T.1    Lane, D.2
  • 8
    • 0030772030 scopus 로고    scopus 로고
    • Reciprocal interference between the sequence-specific core and nonspecific C-terminal DNA binding domains of p53: Implications for regulation
    • Anderson, M.; Woelker, B.; Reed, M.; Wang, P.; Tegtmeyer, P. Reciprocal interference between the sequence-specific core and nonspecific C-terminal DNA binding domains of p53: Implications for regulation. Mol. Cell. Biol. 1997, 17, 6255-6264.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 6255-6264
    • Anderson, M.1    Woelker, B.2    Reed, M.3    Wang, P.4    Tegtmeyer, P.5
  • 9
    • 0026448672 scopus 로고
    • Regulation of the specific DNA binding function of p53
    • Hupp, T.; Meek, D.; Midgley, C.; Lane, D. Regulation of the specific DNA binding function of p53. Cell 1992, 71, 875-886.
    • (1992) Cell , vol.71 , pp. 875-886
    • Hupp, T.1    Meek, D.2    Midgley, C.3    Lane, D.4
  • 10
    • 0037039445 scopus 로고    scopus 로고
    • Human p53 phosphorylation mimic, S392E, increases nonspecific DNA affinity and thermal stability
    • Nichols, N.; Matthews, K. Human p53 phosphorylation mimic, S392E, increases nonspecific DNA affinity and thermal stability. Biochemistry 2002, 41, 170-178.
    • (2002) Biochemistry , vol.41 , pp. 170-178
    • Nichols, N.1    Matthews, K.2
  • 11
    • 0030790778 scopus 로고    scopus 로고
    • Phosphorylation of serine 392 stabilizes the tetramer formation of tumor suppressor protein p53
    • Sakaguchi, K.; Sakamoto, H.; Lewis, M.; Anderson, C.; Erickson, J.; Appella, E.; Xie, D. Phosphorylation of serine 392 stabilizes the tetramer formation of tumor suppressor protein p53. Biochemistry 1997, 36, 10117-10124.
    • (1997) Biochemistry , vol.36 , pp. 10117-10124
    • Sakaguchi, K.1    Sakamoto, H.2    Lewis, M.3    Anderson, C.4    Erickson, J.5    Appella, E.6    Xie, D.7
  • 12
    • 4143146741 scopus 로고    scopus 로고
    • Modification of serine 392 is a critical event in the regulation of p53 nuclear export and stability
    • Kim, Y.; Park, B.; Kim, D.; Kim, W.; Kim, S.; Oh, K.; Lim, J.; Kim, J.; Park, C.; Park, S. Modification of serine 392 is a critical event in the regulation of p53 nuclear export and stability. FEBS Lett. 2004, 572, 92-98.
    • (2004) FEBS Lett , vol.572 , pp. 92-98
    • Kim, Y.1    Park, B.2    Kim, D.3    Kim, W.4    Kim, S.5    Oh, K.6    Lim, J.7    Kim, J.8    Park, C.9    Park, S.10
  • 13
    • 0037217682 scopus 로고    scopus 로고
    • Significance of TP53 mutations in human cancer: A critical analysis of mutations at CpG dinucleotides
    • Soussi, T.; Béroud, C. Significance of TP53 mutations in human cancer: A critical analysis of mutations at CpG dinucleotides. Hum. Mutat. 2003, 21, 192-200.
    • (2003) Hum. Mutat , vol.21 , pp. 192-200
    • Soussi, T.1    Béroud, C.2
  • 14
    • 31044448835 scopus 로고    scopus 로고
    • Linkage between I172N mutation, a marker of 21-hydroxylase deficiency, and a single nucleotide polymorphism in Int6 of CYP21B gene: A genetic study of Sardinian family
    • Concolino, P.; Satta, M.; Santonocito, C.; Carrozza, C.; Rocchetti, S.; Ameglio, F.; Giardina, E.; Zuppi, C.; Capoluongo, E. Linkage between I172N mutation, a marker of 21-hydroxylase deficiency, and a single nucleotide polymorphism in Int6 of CYP21B gene: A genetic study of Sardinian family. Clin. Chim. Acta 2006, 364, 298-302.
    • (2006) Clin. Chim. Acta , vol.364 , pp. 298-302
    • Concolino, P.1    Satta, M.2    Santonocito, C.3    Carrozza, C.4    Rocchetti, S.5    Ameglio, F.6    Giardina, E.7    Zuppi, C.8    Capoluongo, E.9
  • 15
    • 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.; Levine, A.; Nussinov, R. In the quest for stable rescuing mutants of p53: Computational mutagenesis of flexible loop L1. Biochemistry 2005, 44, 1423-1432.
    • (2005) Biochemistry , vol.44 , pp. 1423-1432
    • Pan, Y.1    Ma, B.2    Venkataraghavan, R.3    Levine, A.4    Nussinov, R.5
  • 16
    • 0037343308 scopus 로고    scopus 로고
    • Molecular dynamics of biological macromolecules: A brief history and perspective
    • Karplus, M. Molecular dynamics of biological macromolecules: A brief history and perspective. Biopolymers 2003, 68, 350-358.
    • (2003) Biopolymers , vol.68 , pp. 350-358
    • Karplus, M.1
  • 17
    • 0033945124 scopus 로고    scopus 로고
    • Structure of the negative regulatory domain of p53 bound to S100B(betabeta)
    • Rustandi, R.; Baldisseri, D.; Weber, D. Structure of the negative regulatory domain of p53 bound to S100B(betabeta). Nat. Struct. Biol. 2000, 7, 570-574.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 570-574
    • Rustandi, R.1    Baldisseri, D.2    Weber, D.3
  • 18
    • 4043105578 scopus 로고    scopus 로고
    • Inhibiting S100B restores p53 levels in primary malignant melanoma cancer cells
    • Lin, J.; Yang, Q.; Yan, Z.; Markowitz, J.; Wilder, P.; Carrier, F.; Weber, D. Inhibiting S100B restores p53 levels in primary malignant melanoma cancer cells. J. Biol. Chem. 2004, 279, 34071-34077.
    • (2004) J. Biol. Chem , vol.279 , pp. 34071-34077
    • Lin, J.1    Yang, Q.2    Yan, Z.3    Markowitz, J.4    Wilder, P.5    Carrier, F.6    Weber, D.7
  • 19
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 2008, 9, 40-47.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40-47
    • Zhang, Y.1
  • 20
    • 0026437598 scopus 로고
    • Characterization of the tumor suppressor protein p53 as a protein kinase C substrate and a S100b-binding protein
    • Baudier, J.; Delphin, C.; Grunwald, D.; Khochbin, S.; Lawrence, J. Characterization of the tumor suppressor protein p53 as a protein kinase C substrate and a S100b-binding protein. Proc. Natl. Acad. Sci. USA 1992, 89, 11627-11631.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11627-11631
    • Baudier, J.1    Delphin, C.2    Grunwald, D.3    Khochbin, S.4    Lawrence, J.5
  • 22
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A.; Blundell, T. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234, 779-815.
    • (1993) J. Mol. Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.2
  • 23
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy, R.; Bowie, J.; Eisenberg, D. Assessment of protein models with three-dimensional profiles. Nature 1992, 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.2    Eisenberg, D.3
  • 24
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.; Rullmannn, J.; MacArthur, M.; Kaptein, R.; Thornton, J. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 1996, 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.1    Rullmannn, J.2    Macarthur, M.3    Kaptein, R.4    Thornton, J.5
  • 26
    • 67349279571 scopus 로고    scopus 로고
    • Computational screening and design of S100B ligand to block S100B-p53 interaction
    • Whitlow, J.; Varughese, J.; Zhou, Z.; Bartolotti, L.; Li, Y. Computational screening and design of S100B ligand to block S100B-p53 interaction. J. Mol. Graph. Model. 2009, 27, 969-977.
    • (2009) J. Mol. Graph. Model , vol.27 , pp. 969-977
    • Whitlow, J.1    Varughese, J.2    Zhou, Z.3    Bartolotti, L.4    Li, Y.5
  • 27
    • 54249126941 scopus 로고    scopus 로고
    • Salt-specific stability and denaturation of a short salt-bridge-forming alpha-helix
    • Dzubiella, J. Salt-specific stability and denaturation of a short salt-bridge-forming alpha-helix. J. Am. Chem. Soc. 2008, 130, 14000-14007.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 14000-14007
    • Dzubiella, J.1
  • 28
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy, R.; Bowie, J. U.; Eisenberg, D. Assessment of protein models with three-dimensional profiles. Nature 1992, 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 30
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for Ewald sums in large systems
    • Darden, T.; York, D.; Pedersn, L. Particle mesh Ewald: An N log(N) method for Ewald sums in large systems. J. Chem. Phys. 1993, 98, 10089-10092.
    • (1993) J. Chem. Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersn, L.3
  • 31
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B.; Bekker, H.; Berendsen, H.; Fraaije, J. LINCS: A linear constraint solver for molecular simulations. J. Comput. Chem. 1997, 18, 1463-1472.
    • (1997) J. Comput. Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.3    Fraaije, J.4
  • 32
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W.; Sander, C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.