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Volumn 30, Issue 1, 2001, Pages 75-81

Ser133 phosphate-KIX interactions in the CREB-CBP complex: An ab initio molecular dynamics study

Author keywords

Car Parrinello method; Cyclic AMP response element binding protein; Density functional theory; Low barrier hydrogen bond; Phosphorylation

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; LYSINE; NUCLEAR PROTEIN; PHOSPHOSERINE; TRANSACTIVATOR PROTEIN; TYROSINE;

EID: 0035235378     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490000112     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 0034493839 scopus 로고    scopus 로고
    • Ab initio molecular dynamics studies on HIV-1 reverse transcriptase triphosphate binding site: Implications for nucleoside-analog drug resistance
    • in press
    • Alber F, Carloni P (2000) Ab initio molecular dynamics studies on HIV-1 reverse transcriptase triphosphate binding site: implications for nucleoside-analog drug resistance. Protein Sci (in press)
    • (2000) Protein Sci
    • Alber, F.1    Carloni, P.2
  • 2
    • 0000426945 scopus 로고    scopus 로고
    • Dimethyl phosphate: Stereoelectronic versus environments effects
    • Alber F, Folkers G, Carloni P (1999) Dimethyl phosphate: stereoelectronic versus environments effects. J Phys Chem B 103: 6121-6126
    • (1999) J Phys Chem B , vol.103 , pp. 6121-6126
    • Alber, F.1    Folkers, G.2    Carloni, P.3
  • 4
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behavior
    • Becke AD (1988) Density-functional exchange-energy approximation with correct asymptotic behavior. Phys Rev A 38: 3098-3100
    • (1988) Phys Rev A , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 5
    • 36549100412 scopus 로고
    • A simple measure of electron localization in atomic and molecular systems
    • Becke AD, Edgecombe KE (1990) A simple measure of electron localization in atomic and molecular systems. J Chem Phys 92: 5397-5403
    • (1990) J Chem Phys , vol.92 , pp. 5397-5403
    • Becke, A.D.1    Edgecombe, K.E.2
  • 6
    • 0017411710 scopus 로고    scopus 로고
    • The protein data bank: A computer-based archival file for macromolecular structures
    • Bernstein FCL, Koetzle TF, Williams GJB (1999) The protein data bank: a computer-based archival file for macromolecular structures. J Mol Biol 112: 535-542
    • (1999) J Mol Biol , vol.112 , pp. 535-542
    • Bernstein, F.C.L.1    Koetzle, T.F.2    Williams, G.J.B.3
  • 7
    • 4243606192 scopus 로고
    • Unified approach for molecular dynamics and density-functional theory
    • Car R, Parrinello M (1985) Unified approach for molecular dynamics and density-functional theory. Phys Rev Lett 55: 2471-2474
    • (1985) Phys Rev Lett , vol.55 , pp. 2471-2474
    • Car, R.1    Parrinello, M.2
  • 8
    • 0001416472 scopus 로고    scopus 로고
    • Key steps of the cisplatinDNA interaction: Density functional theory-based molecular dynamics simulations
    • Carloni P, Sprik M, Andreoni W (2000) Key steps of the cisplatinDNA interaction: density functional theory-based molecular dynamics simulations. J Phys Chem 104: 823-835
    • (2000) J Phys Chem , vol.104 , pp. 823-835
    • Carloni, P.1    Sprik, M.2    Andreoni, W.3
  • 10
    • 0028030684 scopus 로고
    • Low-barrier hydrogen bonds and enzymic catalysis
    • Cleland WW, Kreevoy MM (1994) Low-barrier hydrogen bonds and enzymic catalysis. Science 264: 1887-1890
    • (1994) Science , vol.264 , pp. 1887-1890
    • Cleland, W.W.1    Kreevoy, M.M.2
  • 11
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for Ewald sums in large systems
    • Darden, TA, York D (1993) Particle mesh Ewald: an N log(N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10094
    • (1993) J Chem Phys , vol.98 , pp. 10089-10094
    • Darden, T.A.1    York, D.2
  • 12
    • 0032756254 scopus 로고    scopus 로고
    • Serine proteases: An ab initio molecular dynamics study
    • De Santis L, Carloni P (1999) Serine proteases: an ab initio molecular dynamics study. Proteins Struct Funct Genet 37: 611-618
    • (1999) Proteins Struct Funct Genet , vol.37 , pp. 611-618
    • De Santis, L.1    Carloni, P.2
  • 13
    • 0028040716 scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases
    • Frey PA, Whitt SA, Tobin JB (1994) A low-barrier hydrogen bond in the catalytic triad of serine proteases. Science 264: 1927-1930
    • (1994) Science , vol.264 , pp. 1927-1930
    • Frey, P.A.1    Whitt, S.A.2    Tobin, J.B.3
  • 14
    • 12044257628 scopus 로고
    • Covalent nature of the strong homonuclear hydrogen bond. Study of the O-H-O system by crystal structure correlation methods
    • Gilli P, Bertolasi V, Ferretti V, Gilli G (1994) Covalent nature of the strong homonuclear hydrogen bond. Study of the O-H-O system by crystal structure correlation methods. J Am Chem Soc 116:909-915
    • (1994) J Am Chem Soc , vol.116 , pp. 909-915
    • Gilli, P.1    Bertolasi, V.2    Ferretti, V.3    Gilli, G.4
  • 15
    • 0001652762 scopus 로고    scopus 로고
    • Development and assessment of new exchange-correlation functionals
    • Hamprecht FA, Cohen AJ, Tozer DJ, Handy NC (1998) Development and assessment of new exchange-correlation functionals. J Chem Phys 109: 6264-6271
    • (1998) J Chem Phys , vol.109 , pp. 6264-6271
    • Hamprecht, F.A.1    Cohen, A.J.2    Tozer, D.J.3    Handy, N.C.4
  • 16
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch ZS, Tidor B (1994) Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci 3: 211-226
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 17
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distribution
    • Hoover WG (1985) Canonical dynamics: equilibrium phase-space distribution. Phys Rev A 31: 1695-1697
    • (1985) Phys Rev A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 18
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter T, Karin M (1992) The regulation of transcription by phosphorylation. Cell 70: 375-387
    • (1992) Cell , vol.70 , pp. 375-387
    • Hunter, T.1    Karin, M.2
  • 19
    • 10044276520 scopus 로고    scopus 로고
    • Hutter J, Ballone P, Bernasconi N, Focher P, Fois E, Godecker S, Parrinello M, Tuckerman M (1996) CPMD. MPI fur Festkorperforschung and IBM Research Laboratory, Zurich
    • Hutter J, Ballone P, Bernasconi N, Focher P, Fois E, Godecker S, Parrinello M, Tuckerman M (1996) CPMD. MPI fur Festkorperforschung and IBM Research Laboratory, Zurich
  • 20
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • Karplus M, Petsko GA (1990) Molecular dynamics simulations in biology. Nature 347: 631-639
    • (1990) Nature , vol.347 , pp. 631-639
    • Karplus, M.1    Petsko, G.A.2
  • 21
    • 10044263967 scopus 로고    scopus 로고
    • Avatar Software, Stockholm
    • Kraulis P (1997) MolScript v2.1. Avatar Software, Stockholm; www.avatar.se/molscript
    • (1997) MolScript V2.1
    • Kraulis, P.1
  • 24
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • Lee C, Yang W, Parr RG (1988) Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density. Phys Rev B 37: 785-789
    • (1988) Phys Rev B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 25
    • 0029030233 scopus 로고
    • Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
    • Lumb KJ, Kim PS (1995) Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science 268: 436-439
    • (1995) Science , vol.268 , pp. 436-439
    • Lumb, K.J.1    Kim, P.S.2
  • 26
    • 0026592667 scopus 로고
    • Crystal structure of the complex between carboxypeptidase A and the byproduct analog inhibitor L-benzylsuccinate at 2.0 Å resolution
    • Mangani S, Carloni P, Orioli P (1992) Crystal structure of the complex between carboxypeptidase A and the byproduct analog inhibitor L-benzylsuccinate at 2.0 Å resolution. J Mol Biol 223: 573-578
    • (1992) J Mol Biol , vol.223 , pp. 573-578
    • Mangani, S.1    Carloni, P.2    Orioli, P.3
  • 27
    • 4243690324 scopus 로고    scopus 로고
    • Maximally-localized Wannier functions for composite energy bands
    • Marzari N, Vanderbilt D (1997) Maximally-localized Wannier functions for composite energy bands. Phys Rev B 56: 12847-12865
    • (1997) Phys Rev B , vol.56 , pp. 12847-12865
    • Marzari, N.1    Vanderbilt, D.2
  • 28
    • 9144240095 scopus 로고
    • Dreiding: A generic force field for molecular simulations
    • Mayo SL, Olafson BD, Goddard WA (1990) Dreiding: a generic force field for molecular simulations. J Phys Chem 94: 8897-8909
    • (1990) J Phys Chem , vol.94 , pp. 8897-8909
    • Mayo, S.L.1    Olafson, B.D.2    Goddard, W.A.3
  • 29
    • 0032982862 scopus 로고    scopus 로고
    • Electrostatic contribution of phosphorylation to the stability of the CREB-CBP activator-coactivator complex
    • Mestas SP, Lumb KJ (1999) Electrostatic contribution of phosphorylation to the stability of the CREB-CBP activator-coactivator complex. Nat Struct Biol 6: 613-614
    • (1999) Nat Struct Biol , vol.6 , pp. 613-614
    • Mestas, S.P.1    Lumb, K.J.2
  • 30
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • Nosé SJ (1984) A unified formulation of the constant temperature molecular dynamics methods. J Chem Phys 81: 511-519
    • (1984) J Chem Phys , vol.81 , pp. 511-519
    • Nosé, S.J.1
  • 32
    • 0033998647 scopus 로고    scopus 로고
    • Conformational flexibility of the catalytic asp dyad in HIV-1 protease: An ab initio study on the free enzyme
    • Piana S, Carloni P (2000) Conformational flexibility of the catalytic asp dyad in HIV-1 protease: an ab initio study on the free enzyme. Proteins 39: 26-36
    • (2000) Proteins , vol.39 , pp. 26-36
    • Piana, S.1    Carloni, P.2
  • 33
    • 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 GC, Parker D, Dyson HJ, Montminy MR, Wright PE (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
  • 35
    • 0030443476 scopus 로고    scopus 로고
    • Geometry of the phosphate group and its interactions with metal cations in crystals and ab initio calculations
    • Schneider B, Kabelac M, Hobza P (1996) Geometry of the phosphate group and its interactions with metal cations in crystals and ab initio calculations. J Am Chem Soc 118: 12207-12217
    • (1996) J Am Chem Soc , vol.118 , pp. 12207-12217
    • Schneider, B.1    Kabelac, M.2    Hobza, P.3
  • 36
    • 18344379950 scopus 로고
    • Water molecular dipole in the gas and in the liquid phase
    • Silvestrelli PL, Parrinello M (1990) Water molecular dipole in the gas and in the liquid phase. Phys Rev Lett 82: 3308-3311
    • (1990) Phys Rev Lett , vol.82 , pp. 3308-3311
    • Silvestrelli, P.L.1    Parrinello, M.2
  • 37
    • 0032066447 scopus 로고    scopus 로고
    • Maximally-localized Wannier functions for disordered systems: Application to amorphous silicon
    • Silvestrelli PL, Marzari N, Vanderbilt D, Parrinello M (1998) Maximally-localized Wannier functions for disordered systems: application to amorphous silicon. Solid State Commun 107: 7-11
    • (1998) Solid State Commun , vol.107 , pp. 7-11
    • Silvestrelli, P.L.1    Marzari, N.2    Vanderbilt, D.3    Parrinello, M.4
  • 38
    • 0027946619 scopus 로고
    • Classification of chemical bonds based on topological analysis of electron localization functions
    • Silvi B, Savin A (1994) Classification of chemical bonds based on topological analysis of electron localization functions. Nature 371: 683-686
    • (1994) Nature , vol.371 , pp. 683-686
    • Silvi, B.1    Savin, A.2
  • 39
    • 0000983566 scopus 로고    scopus 로고
    • Hydrogenbonding in glycine and malonaldehyde: Performance of the Lapl correlation functional
    • Sirois S, Proynov EI, Nguyen DT, Salahub DR (1997) Hydrogenbonding in glycine and malonaldehyde: performance of the Lapl correlation functional. J Chem Phys 107: 6770-6781.
    • (1997) J Chem Phys , vol.107 , pp. 6770-6781
    • Sirois, S.1    Proynov, E.I.2    Nguyen, D.T.3    Salahub, D.R.4
  • 40
    • 0030284229 scopus 로고    scopus 로고
    • Ab initio molecular dynamics simulation of liquids and solutions
    • Sprik M (1996) Ab initio molecular dynamics simulation of liquids and solutions. J Phys Condens Matter 8: 9405-9409
    • (1996) J Phys Condens Matter , vol.8 , pp. 9405-9409
    • Sprik, M.1
  • 41
    • 33645426115 scopus 로고
    • Efficient pseudopotentials for planewave calculation
    • Troullier N, Martins JL (1991) Efficient pseudopotentials for planewave calculation. Phys Rev B 43: 1943-2006
    • (1991) Phys Rev B , vol.43 , pp. 1943-2006
    • Troullier, N.1    Martins, J.L.2
  • 42
    • 0030031374 scopus 로고    scopus 로고
    • Molecular dynamics investigation of the structure of a fully hydrated gel-phase dipalmitoylphosphatidylcholine bilayer
    • Tu K, Tobias DJ, Blasie JK, Klein ML (1996) Molecular dynamics investigation of the structure of a fully hydrated gel-phase dipalmitoylphosphatidylcholine bilayer. Biophys J 70: 595-608
    • (1996) Biophys J , vol.70 , pp. 595-608
    • Tu, K.1    Tobias, D.J.2    Blasie, J.K.3    Klein, M.L.4


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