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Volumn 56, Issue 2, 2004, Pages 322-337

Change in protein flexibility upon complex formation: Analysis of Ras-Raf using molecular dynamics and a molecular framework approach

Author keywords

Allostery; Conformational change; Correlated motions; FIRST; Flexibility rigidity; Induced fit; Mobility dynamics; Protein protein interactions

Indexed keywords

RAF PROTEIN; RAS PROTEIN;

EID: 3042806330     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20116     Document Type: Article
Times cited : (107)

References (106)
  • 1
    • 3042828688 scopus 로고
    • Protein flexibility in enzyme action and enzyme control
    • Koshland DE. Protein flexibility in enzyme action and enzyme control. Science 1967;156:540.
    • (1967) Science , vol.156 , pp. 540
    • Koshland, D.E.1
  • 2
    • 0026720247 scopus 로고
    • Crystalline ribonuclease A loses function below the dynamical transition at 220 K
    • Rasmussen BF, Stock AM, Ringe D, Petsko GA. Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature 1992;357:423-424.
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B.F.1    Stock, A.M.2    Ringe, D.3    Petsko, G.A.4
  • 3
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering
    • Ferrand M, Dianoux AJ, Petry W, Zaccai G. Thermal motions and function of bacteriorhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering. Proc Natl Acad Sci USA 1993;90:9668-9672.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9668-9672
    • Ferrand, M.1    Dianoux, A.J.2    Petry, W.3    Zaccai, G.4
  • 4
    • 0036193327 scopus 로고    scopus 로고
    • Temperature dependence of protein dynamics: Computer simulation analysis of neutron scattering properties
    • Hayward JA, Smith JC. Temperature dependence of protein dynamics: computer simulation analysis of neutron scattering properties. Biophys J 2002;82:1216-1225.
    • (2002) Biophys J , vol.82 , pp. 1216-1225
    • Hayward, J.A.1    Smith, J.C.2
  • 5
    • 0031758464 scopus 로고    scopus 로고
    • Native protein fluctuations: The conformational-motion temperature and the inverse correlation of protein flexibility with protein stability
    • Tang KE, Dill KA. Native protein fluctuations: the conformational-motion temperature and the inverse correlation of protein flexibility with protein stability. J Biomol Struct Dyn 1998;16:397-411.
    • (1998) J Biomol Struct Dyn , vol.16 , pp. 397-411
    • Tang, K.E.1    Dill, K.A.2
  • 6
    • 0028361031 scopus 로고
    • Accuracy of protein flexibility predictions
    • Vihinen M, Torkkila E, Riikonen P. Accuracy of protein flexibility predictions. Proteins 1994;19:141-149.
    • (1994) Proteins , vol.19 , pp. 141-149
    • Vihinen, M.1    Torkkila, E.2    Riikonen, P.3
  • 7
    • 0036385839 scopus 로고    scopus 로고
    • Elastic properties of proteins: Insight on the folding process and evolutionary selection of native structures
    • Micheletti C, Lattanzi G, Maritan A. Elastic properties of proteins: insight on the folding process and evolutionary selection of native structures. J Mol Biol 2002;321:909-921.
    • (2002) J Mol Biol , vol.321 , pp. 909-921
    • Micheletti, C.1    Lattanzi, G.2    Maritan, A.3
  • 8
    • 0035827364 scopus 로고    scopus 로고
    • Protein dynamics, folding, and misfolding: From basic physical chemistry to human conformational diseases
    • Ferreira ST, De Felice FG. Protein dynamics, folding, and misfolding: from basic physical chemistry to human conformational diseases. FEBS Lett 2001;498:129-134.
    • (2001) FEBS Lett , vol.498 , pp. 129-134
    • Ferreira, S.T.1    De Felice, F.G.2
  • 10
    • 0030707656 scopus 로고    scopus 로고
    • Structural plasticity in a remodeled protein-protein interface
    • Atwell S, Ultsch M, De Vos AM, Wells JA. Structural plasticity in a remodeled protein-protein interface. Science 1997;278:1125-1128.
    • (1997) Science , vol.278 , pp. 1125-1128
    • Atwell, S.1    Ultsch, M.2    De Vos, A.M.3    Wells, J.A.4
  • 12
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano WL, Ultsch MH, de Vos AM, Wells JA. Convergent solutions to binding at a protein-protein interface. Science 2000;287:1279-1283.
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 14
    • 0034710976 scopus 로고    scopus 로고
    • Can allosteric regulation be predicted from structure?
    • Freire E. Can allosteric regulation be predicted from structure? Proc Natl Acad Sci USA 2000;97:11680-11682.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11680-11682
    • Freire, E.1
  • 15
    • 0034710950 scopus 로고    scopus 로고
    • Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble
    • Pan H, Lee JC, Hilser VJ. Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble. Proc Natl Acad Sci USA 2000;97:12020-12025.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12020-12025
    • Pan, H.1    Lee, J.C.2    Hilser, V.J.3
  • 16
    • 0029764317 scopus 로고    scopus 로고
    • Backbone dynamics of the C-terminal domain of Escherichia coli topoisomerase I in the absence and presence of single-stranded DNA
    • Yu L, Zhu CX, Tse-Dinh YC, Fesik SW. Backbone dynamics of the C-terminal domain of Escherichia coli topoisomerase I in the absence and presence of single-stranded DNA. Biochemistry 1996;35:9661-9666.
    • (1996) Biochemistry , vol.35 , pp. 9661-9666
    • Yu, L.1    Zhu, C.X.2    Tse-Dinh, Y.C.3    Fesik, S.W.4
  • 17
    • 0031001259 scopus 로고    scopus 로고
    • Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide
    • Olejniczak ET, Zhou MM, Fesik SW. Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide. Biochemistry 1997;36:4118-4124.
    • (1997) Biochemistry , vol.36 , pp. 4118-4124
    • Olejniczak, E.T.1    Zhou, M.M.2    Fesik, S.W.3
  • 18
    • 0032710610 scopus 로고    scopus 로고
    • Increased protein backbone conformational entropy upon hydrophobic ligand binding
    • Zidek L, Novotny MV, Stone MJ. Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nat Struct Biol 1999;6:1118-1121.
    • (1999) Nat Struct Biol , vol.6 , pp. 1118-1121
    • Zidek, L.1    Novotny, M.V.2    Stone, M.J.3
  • 19
    • 0035901519 scopus 로고    scopus 로고
    • An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs
    • Loh AP, Pawley N, Nicholson LK, Oswald RE. An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs. Biochemistry 2001;40:4590-4600.
    • (2001) Biochemistry , vol.40 , pp. 4590-4600
    • Loh, A.P.1    Pawley, N.2    Nicholson, L.K.3    Oswald, R.E.4
  • 20
    • 0037470616 scopus 로고    scopus 로고
    • Increased backbone mobility in β-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3
    • Arumugam S, Gao G, Patton BL, Semenchenko V, Brew K, Van Doren SR. Increased backbone mobility in β-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3. J Mol Biol 2003;327:719-734.
    • (2003) J Mol Biol , vol.327 , pp. 719-734
    • Arumugam, S.1    Gao, G.2    Patton, B.L.3    Semenchenko, V.4    Brew, K.5    Van Doren, S.R.6
  • 21
    • 0032756923 scopus 로고    scopus 로고
    • The "dynamics" in the thermodynamics of binding
    • Forman-Kay JD. The "dynamics" in the thermodynamics of binding. Nat Struct Biol 1999;6:1086-1087.
    • (1999) Nat Struct Biol , vol.6 , pp. 1086-1087
    • Forman-Kay, J.D.1
  • 23
    • 0030042698 scopus 로고    scopus 로고
    • Correlation between dynamics and high affinity binding in an SH2 domain interaction
    • Kay LE, Muhandiram DR, Farrow NA, Aubin Y, Forman-Kay JD. Correlation between dynamics and high affinity binding in an SH2 domain interaction. Biochemistry 1996;35:361-368.
    • (1996) Biochemistry , vol.35 , pp. 361-368
    • Kay, L.E.1    Muhandiram, D.R.2    Farrow, N.A.3    Aubin, Y.4    Forman-Kay, J.D.5
  • 24
    • 0001666112 scopus 로고
    • Entropy changes accompanying association reactions of proteins
    • Steinberg IZ, Scheraga HA. Entropy changes accompanying association reactions of proteins. J Biol Chem 1963;238:172-181.
    • (1963) J Biol Chem , vol.238 , pp. 172-181
    • Steinberg, I.Z.1    Scheraga, H.A.2
  • 25
    • 0030299991 scopus 로고    scopus 로고
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: Backbone dynamics and entropy changes of an enzyme upon inhibitor binding
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: Backbone dynamics and entropy changes of an enzyme upon inhibitor binding. Biochemistry 1996;35:16036-16047.
    • (1996) Biochemistry , vol.35 , pp. 16036-16047
    • Stivers, J.T.1    Abeygunawardana, C.2    Mildvan, A.S.3    Whitman, C.P.4
  • 26
    • 0031043596 scopus 로고    scopus 로고
    • Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange
    • Hodsdon ME, Cistola DP. Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange. Biochemistry 1997;36:2278-2290.
    • (1997) Biochemistry , vol.36 , pp. 2278-2290
    • Hodsdon, M.E.1    Cistola, D.P.2
  • 27
    • 0033988897 scopus 로고    scopus 로고
    • Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex
    • Lee AL, Kinnear SA, Wand AJ. Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex. Nat Struct Biol 2000;7:72-77.
    • (2000) Nat Struct Biol , vol.7 , pp. 72-77
    • Lee, A.L.1    Kinnear, S.A.2    Wand, A.J.3
  • 28
    • 0036904038 scopus 로고    scopus 로고
    • Changes in flexibility upon binding: Application of the self-consistent pair contact probability method to protein-protein interactions
    • Canino LS, Shen T, McCammon JA. Changes in flexibility upon binding: application of the self-consistent pair contact probability method to protein-protein interactions. J Chem Phys 2002;117:9927-9933.
    • (2002) J Chem Phys , vol.117 , pp. 9927-9933
    • Canino, L.S.1    Shen, T.2    McCammon, J.A.3
  • 29
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai C-J, Kumar S, Ma B, Nussinov R. Folding funnels, binding funnels, and protein function. Protein Sci 1999;8:1181-1190.
    • (1999) Protein Sci , vol.8 , pp. 1181-1190
    • Tsai, C.-J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 30
    • 0033621104 scopus 로고    scopus 로고
    • Folding and binding cascades: Shifts in energy landscapes
    • Tsai C-J, Ma B, Nussinov R. Folding and binding cascades: Shifts in energy landscapes. Proc Natl Acad Sci USA 1999;96:9970-9972.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9970-9972
    • Tsai, C.-J.1    Ma, B.2    Nussinov, R.3
  • 31
    • 0029159748 scopus 로고
    • Rigid domains in proteins: An algorithmic approach to their identification
    • Nichols WL, Rose GD, Ten Eyck LF, Zimm BH. Rigid domains in proteins: An algorithmic approach to their identification. Proteins 1995;23:38-48.
    • (1995) Proteins , vol.23 , pp. 38-48
    • Nichols, W.L.1    Rose, G.D.2    Ten Eyck, L.F.3    Zimm, B.H.4
  • 32
    • 0028943588 scopus 로고
    • Continuous and discontinuous domains: An algorithm for the automatic generation of reliable protein domain definitions
    • Siddiqui AS, Barton GJ. Continuous and discontinuous domains: an algorithm for the automatic generation of reliable protein domain definitions. Protein Sci 1995;4:872-884.
    • (1995) Protein Sci , vol.4 , pp. 872-884
    • Siddiqui, A.S.1    Barton, G.J.2
  • 33
    • 0028826992 scopus 로고
    • Automatic analysis of protein conformational changes by multiple linkage clustering
    • Boutonnet NS, Rooman MJ, Wodak SJ. Automatic analysis of protein conformational changes by multiple linkage clustering. J. Mol. Biol. 1995;253:633-647.
    • (1995) J Mol Biol , vol.253 , pp. 633-647
    • Boutonnet, N.S.1    Rooman, M.J.2    Wodak, S.J.3
  • 34
    • 0034655949 scopus 로고    scopus 로고
    • The morph server: A standardized system for analyzing and visualizing macromolecular motions in a database framework
    • Krebs WG, Gerstein M. The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework. Nucleic Acids Research 2000;28:1665-1675.
    • (2000) Nucleic Acids Research , vol.28 , pp. 1665-1675
    • Krebs, W.G.1    Gerstein, M.2
  • 35
    • 0036681439 scopus 로고    scopus 로고
    • Flexible protein alignment and hinge detection
    • Shatsky M, Nussinov R, Wolfson HJ. Flexible protein alignment and hinge detection. Proteins 2002;48:242-256.
    • (2002) Proteins , vol.48 , pp. 242-256
    • Shatsky, M.1    Nussinov, R.2    Wolfson, H.J.3
  • 36
    • 0028290005 scopus 로고
    • Parser for protein folding units
    • Holm L, Sander C. Parser for protein folding units. Proteins 1994;19:256-268.
    • (1994) Proteins , vol.19 , pp. 256-268
    • Holm, L.1    Sander, C.2
  • 37
    • 0023055758 scopus 로고
    • Compact units in proteins
    • Zehfus MH, Rose GD. Compact units in proteins. Biochemistry 1986;25:5759-5765.
    • (1986) Biochemistry , vol.25 , pp. 5759-5765
    • Zehfus, M.H.1    Rose, G.D.2
  • 38
    • 0021918946 scopus 로고
    • Prediction of chain flexibility in proteins
    • Karplus PA, Schulz GE. Prediction of chain flexibility in proteins. Naturwissenschaften 1985;72:212-213.
    • (1985) Naturwissenschaften , vol.72 , pp. 212-213
    • Karplus, P.A.1    Schulz, G.E.2
  • 39
    • 0030939896 scopus 로고    scopus 로고
    • A new method for modeling large-scale rearrangements of protein domains
    • Maiorov V, Abagyan R. A new method for modeling large-scale rearrangements of protein domains. Proteins 1997;27:410-424.
    • (1997) Proteins , vol.27 , pp. 410-424
    • Maiorov, V.1    Abagyan, R.2
  • 40
    • 0000516026 scopus 로고    scopus 로고
    • Molecular dynamics and normal mode analysis of biomolecular rigidity
    • Thorpe MF, Duxbury PM, eds. New York: Kluwer Academic/Plenum Publishers
    • Case DA. Molecular dynamics and normal mode analysis of biomolecular rigidity. In: Thorpe MF, Duxbury PM, eds. Rigidity Theory and Applications. New York: Kluwer Academic/Plenum Publishers; 1999. pp 329-344.
    • (1999) Rigidity Theory and Applications , pp. 329-344
    • Case, D.A.1
  • 41
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar I, Atilgan AR, Erman B. Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Fold Des 1997;2:173-181.
    • (1997) Fold Des , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 43
    • 0037062479 scopus 로고    scopus 로고
    • Domain movements in human fatty acid synthase by quantized elastic deformational model
    • Ming D, Kong Y, Wakil SJ, Brink J, Ma J. Domain movements in human fatty acid synthase by quantized elastic deformational model. Proc Nat Acad Sci USA 2002;99:7895-7899.
    • (2002) Proc Nat Acad Sci USA , vol.99 , pp. 7895-7899
    • Ming, D.1    Kong, Y.2    Wakil, S.J.3    Brink, J.4    Ma, J.5
  • 44
    • 0036382958 scopus 로고    scopus 로고
    • Exploring global distortions of biological macromolecules and assemblies from low-resolution structural information and elastic network theory
    • Tama F, Wriggers W, Brooks CL, 3rd. Exploring global distortions of biological macromolecules and assemblies from low-resolution structural information and elastic network theory. J Mol Biol 2002;321:297-305.
    • (2002) J Mol Biol , vol.321 , pp. 297-305
    • Tama, F.1    Wriggers, W.2    Brooks III, C.L.3
  • 45
    • 0037022347 scopus 로고    scopus 로고
    • Flexibility and packing in proteins
    • Halle B. Flexibility and packing in proteins. Proc Natl Acad Sci USA 2002;99:1274-1279.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1274-1279
    • Halle, B.1
  • 47
    • 0001766636 scopus 로고
    • On the calculation of the equilibrium and stiffness of frames
    • Maxwell JC. On the calculation of the equilibrium and stiffness of frames. Philos Mag 1864;27:294-299.
    • (1864) Philos Mag , vol.27 , pp. 294-299
    • Maxwell, J.C.1
  • 48
    • 0000311742 scopus 로고    scopus 로고
    • Generic rigidity of network glasses
    • Thorpe MF, Duxbury PM, eds. New York: Kluwer Academic/Plenum Publishers
    • Thorpe MF, Jacobs DJ, Chubynsky NV, Rader AJ. Generic rigidity of network glasses. In: Thorpe MF, Duxbury PM, eds. Rigidity theory and applications. New York: Kluwer Academic/Plenum Publishers; 1999. pp 239-277.
    • (1999) Rigidity Theory and Applications , pp. 239-277
    • Thorpe, M.F.1    Jacobs, D.J.2    Chubynsky, N.V.3    Rader, A.J.4
  • 49
    • 0014856102 scopus 로고
    • On graphs and rigidity of plane skeletal structures
    • Laman G. On graphs and rigidity of plane skeletal structures. J Eng Math 1970;4:331-340.
    • (1970) J Eng Math , vol.4 , pp. 331-340
    • Laman, G.1
  • 50
    • 0002883806 scopus 로고
    • Recent advances in generic rigidity of structures
    • Tay T-S, Whiteley W. Recent advances in generic rigidity of structures. Struct Topol 1985;9:31-38.
    • (1985) Struct Topol , vol.9 , pp. 31-38
    • Tay, T.-S.1    Whiteley, W.2
  • 51
    • 0003096681 scopus 로고    scopus 로고
    • Flexible and rigid regions in proteins
    • Thorpe MF, Duxbury PM, eds. New York: Kluwer Academic/Plenum Publishers
    • Jacobs DJ, Kuhn LA, Thorpe MF. Flexible and rigid regions in proteins. In: Thorpe MF, Duxbury PM, eds. Rigidity theory and applications. New York: Kluwer Academic/Plenum Publishers; 1999.
    • (1999) Rigidity Theory and Applications
    • Jacobs, D.J.1    Kuhn, L.A.2    Thorpe, M.F.3
  • 52
    • 0000785338 scopus 로고
    • Generic rigidity percolation: The pebble game
    • Jacobs DJ, Thorpe MF. Generic rigidity percolation: The pebble game. Phys Rev Lett 1995;75:4051-4054.
    • (1995) Phys Rev Lett , vol.75 , pp. 4051-4054
    • Jacobs, D.J.1    Thorpe, M.F.2
  • 53
    • 0031281604 scopus 로고    scopus 로고
    • An algorithm for two dimensional rigidity percolation: The pebble game
    • Jacobs DJ, Hendrickson B. An algorithm for two dimensional rigidity percolation: The pebble game. J Comput Phys 1997;137:346-365.
    • (1997) J Comput Phys , vol.137 , pp. 346-365
    • Jacobs, D.J.1    Hendrickson, B.2
  • 54
    • 0000785337 scopus 로고    scopus 로고
    • Generic rigidity percolation in two dimensions
    • Jacobs DJ, Thorpe MF. Generic rigidity percolation in two dimensions. Phys Rev E 1996;53:3683-3693.
    • (1996) Phys Rev E , vol.53 , pp. 3683-3693
    • Jacobs, D.J.1    Thorpe, M.F.2
  • 56
    • 0035427398 scopus 로고    scopus 로고
    • Protein flexibility predictions using graph theory
    • Jacobs DJ, Rader AJ, Kuhn LA, Thorpe MF. Protein flexibility predictions using graph theory. Proteins 2001;44:150-165.
    • (2001) Proteins , vol.44 , pp. 150-165
    • Jacobs, D.J.1    Rader, A.J.2    Kuhn, L.A.3    Thorpe, M.F.4
  • 57
    • 0036888379 scopus 로고    scopus 로고
    • Identifying protein folding cores from the evolution of flexible regions during unfolding
    • Hespenheide BM, Rader AJ, Thorpe MF, Kuhn LA. Identifying protein folding cores from the evolution of flexible regions during unfolding. J Mol Graph Model 2002;21:195-207.
    • (2002) J Mol Graph Model , vol.21 , pp. 195-207
    • Hespenheide, B.M.1    Rader, A.J.2    Thorpe, M.F.3    Kuhn, L.A.4
  • 59
    • 0034605862 scopus 로고    scopus 로고
    • Ras - A molecular switch involved in tumor formation
    • Wittinghofer A, Waldmann H. Ras - a molecular switch involved in tumor formation. Angew Chem Int Ed Engl 2000;39:4193-4214.
    • (2000) Angew Chem Int Ed Engl , vol.39 , pp. 4193-4214
    • Wittinghofer, A.1    Waldmann, H.2
  • 60
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang SR. G protein mechanisms: insights from structural analysis. Annu Rev Biochem 1997;66:639-678.
    • (1997) Annu Rev Biochem , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 61
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic Ras proteins
    • Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic Ras proteins. Science 1990;247:939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    DeVos, A.M.3    Brunger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 62
    • 0030464444 scopus 로고    scopus 로고
    • How Ras-related proteins talk to their effectors
    • Wittinghofer A, Nassar N. How Ras-related proteins talk to their effectors. Trends Biochem Sci 1996;21:488-491.
    • (1996) Trends Biochem Sci , vol.21 , pp. 488-491
    • Wittinghofer, A.1    Nassar, N.2
  • 64
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the Ha-Ras oncogene product p21 in the triphosphate conformation
    • Pai EF, Kabsch W, Krengel U, Holmes KC, John J, Wittinghofer A. Structure of the guanine-nucleotide-binding domain of the Ha-Ras oncogene product p21 in the triphosphate conformation. Nature 1989;341:209-214.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 65
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-Ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-Ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J 1990;9:2351-2359.
    • (1990) EMBO J , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 66
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A. The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 1995;375:554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 68
    • 53249121746 scopus 로고    scopus 로고
    • Molecular dynamics on complexes of Ras-p21 and its inhibitor protein, Rap-1A, bound to the Ras-binding domain of the Raf-p74 protein: Identification of effector domains in the Raf protein
    • Chen JM, Monaco R, Manolatos S, Brandt-Rauf PW, Friedman FK, Pincus MR. Molecular dynamics on complexes of Ras-p21 and its inhibitor protein, Rap-1A, bound to the Ras-binding domain of the Raf-p74 protein: Identification of effector domains in the Raf protein. J Protein Chem 1997;16:619-629.
    • (1997) J Protein Chem , vol.16 , pp. 619-629
    • Chen, J.M.1    Monaco, R.2    Manolatos, S.3    Brandt-Rauf, P.W.4    Friedman, F.K.5    Pincus, M.R.6
  • 69
    • 0033120983 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the Ras:Raf and Rap:Raf complexes
    • Zeng J, Treutlein HR, Simonson T. Molecular dynamics simulations of the Ras:Raf and Rap:Raf complexes. Proteins 1999;35:89-100.
    • (1999) Proteins , vol.35 , pp. 89-100
    • Zeng, J.1    Treutlein, H.R.2    Simonson, T.3
  • 70
    • 0032080535 scopus 로고    scopus 로고
    • Conformation of the Ras-binding domain of Raf studied by molecular dynamics and free energy simulations
    • Zeng J, Treutlein HR, Simonson T. Conformation of the Ras-binding domain of Raf studied by molecular dynamics and free energy simulations. Proteins 1998;31:186-200.
    • (1998) Proteins , vol.31 , pp. 186-200
    • Zeng, J.1    Treutlein, H.R.2    Simonson, T.3
  • 71
    • 0032898393 scopus 로고    scopus 로고
    • Protein-protein recognition: An experimental and computational study of the R89K mutation in Raf and its effect on Ras binding
    • Zeng J, Fridman M, Maruta H, Treutlein HR, Simonson T. Protein-protein recognition: an experimental and computational study of the R89K mutation in Raf and its effect on Ras binding. Protein Sci 1999;8:50-64.
    • (1999) Protein Sci , vol.8 , pp. 50-64
    • Zeng, J.1    Fridman, M.2    Maruta, H.3    Treutlein, H.R.4    Simonson, T.5
  • 72
    • 0032031405 scopus 로고    scopus 로고
    • Electrostatic contributions to protein-protein binding affinities: Application to Rap/Raf interaction
    • Muegge I, Schweins T, Warshel A. Electrostatic contributions to protein-protein binding affinities: application to Rap/Raf interaction. Proteins 1998;30:407-423.
    • (1998) Proteins , vol.30 , pp. 407-423
    • Muegge, I.1    Schweins, T.2    Warshel, A.3
  • 73
    • 53249121746 scopus 로고    scopus 로고
    • Molecular dynamics on complexes of Ras-p21 and its inhibitor protein, Rap-1A, bound to the Ras-binding domain of the Raf-p74 protein: Identification of effector domains in the Raf protein
    • Chen JM, Monaco R, Manolatos S, Brandt-Rauf PW, Friedman FK, Pincus MR. Molecular dynamics on complexes of Ras-p21 and its inhibitor protein, Rap-1A, bound to the Ras-binding domain of the Raf-p74 protein: identification of effector domains in the Raf protein. J Protein Chem 1997;16:619-629.
    • (1997) J Protein Chem , vol.16 , pp. 619-629
    • Chen, J.M.1    Monaco, R.2    Manolatos, S.3    Brandt-Rauf, P.W.4    Friedman, F.K.5    Pincus, M.R.6
  • 74
    • 0034469856 scopus 로고    scopus 로고
    • Identification, using molecular dynamics, of an effector domain of the Ras-binding domain of the Raf-p74 protein that is uniquely involved in oncogenic Ras-p21 signaling
    • Chen JM, Rijhwani K, Friedman FK, Hyde MJ, Pincus MR. Identification, using molecular dynamics, of an effector domain of the Ras-binding domain of the Raf-p74 protein that is uniquely involved in oncogenic Ras-p21 signaling. J Protein Chem 2000;19:545-551.
    • (2000) J Protein Chem , vol.19 , pp. 545-551
    • Chen, J.M.1    Rijhwani, K.2    Friedman, F.K.3    Hyde, M.J.4    Pincus, M.R.5
  • 75
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • Gohlke H, Kiel C, Case DA. Insights into protein-protein binding by free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J Mol Biol 2003;330:891-913.
    • (2003) J Mol Biol , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 76
    • 3042713344 scopus 로고    scopus 로고
    • Case DA, Pearlman DA, Caldwell JW, Cheatham III TE, Wang J, Ross WS, Simmerling CL, Darden TA, Merz KM, Stanton RV, Cheng AL, Vincent JJ, Crowley M, Tsui V, Gohlke H, Radmer RJ, Duan Y, Pitera J, Massova I, Seibel GL, Singh UC, Weiner PK, Kollman PA, Amber F. University of California: San Francisco, 2002
    • Case DA, Pearlman DA, Caldwell JW, Cheatham III TE, Wang J, Ross WS, Simmerling CL, Darden TA, Merz KM, Stanton RV, Cheng AL, Vincent JJ, Crowley M, Tsui V, Gohlke H, Radmer RJ, Duan Y, Pitera J, Massova I, Seibel GL, Singh UC, Weiner PK, Kollman PA, Amber F. University of California: San Francisco, 2002.
  • 78
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen WL, Chandrasekhar J, Madura J, Klein ML. Comparison of simple potential functions for simulating liquid water. J Chem Phys 1983;79:926-935.
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.3    Klein, M.L.4
  • 80
    • 84986468955 scopus 로고
    • A molecular dynamics study of the inhibition of chicken dihydrofolate reductase by a phenyl triazine
    • Leach AR, Klein TE. A molecular dynamics study of the inhibition of chicken dihydrofolate reductase by a phenyl triazine. J Comput Chem 1995;16:1378-1393.
    • (1995) J Comput Chem , vol.16 , pp. 1378-1393
    • Leach, A.R.1    Klein, T.E.2
  • 81
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for determining atom-centered charges: The RESP model
    • Bayly CI, Cieplak P, Cornell WD, Kollman PA. A well-behaved electrostatic potential based method using charge restraints for determining atom-centered charges: The RESP model. J Phys Chem 1993;97:10269-10280.
    • (1993) J Phys Chem , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 82
    • 3042837801 scopus 로고
    • Modeling ion ligand interactions in solutions and biomolecules
    • Aqvist J. Modeling ion ligand interactions in solutions and biomolecules. Theochem J Mol Struct 1992;88:135-152.
    • (1992) Theochem J Mol Struct , vol.88 , pp. 135-152
    • Aqvist, J.1
  • 84
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye T, Karplus M. Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins 1991;11:205-217.
    • (1991) Proteins , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2
  • 85
    • 0032546743 scopus 로고    scopus 로고
    • Are there non-trivial dynamic cross-correlations in proteins?
    • Abseher R, Nilges M. Are there non-trivial dynamic cross-correlations in proteins? J Mol Biol 1998;279:911-920.
    • (1998) J Mol Biol , vol.279 , pp. 911-920
    • Abseher, R.1    Nilges, M.2
  • 86
    • 0029092698 scopus 로고
    • Fluctuation and cross-correlation analysis of protein motions observed in nanosecond molecular dynamics simulations
    • Hunenberger PH, Mark AE, van Gunsteren WF. Fluctuation and cross-correlation analysis of protein motions observed in nanosecond molecular dynamics simulations. J Mol Biol 1995;252:492-503.
    • (1995) J Mol Biol , vol.252 , pp. 492-503
    • Hunenberger, P.H.1    Mark, A.E.2    Van Gunsteren, W.F.3
  • 87
    • 0030601771 scopus 로고    scopus 로고
    • Comment on a "fluctuation and cross correlation analysis of protein motions observed in nanosecond molecular dynamics simulations"
    • Karplus M, Ichiye T. Comment on a "fluctuation and cross correlation analysis of protein motions observed in nanosecond molecular dynamics simulations" J Mol Biol 1996;263:120-122.
    • (1996) J Mol Biol , vol.263 , pp. 120-122
    • Karplus, M.1    Ichiye, T.2
  • 88
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: Summaries and analyses of PDB structures
    • Laskowski RA. PDBsum: summaries and analyses of PDB structures. Nucl Acid Res 2001;29:221-222.
    • (2001) Nucl Acid Res , vol.29 , pp. 221-222
    • Laskowski, R.A.1
  • 89
    • 0343742614 scopus 로고    scopus 로고
    • Automated design of the surface positions of protein helices
    • Dahiyat BI, Gordon DB, Mayo SL. Automated design of the surface positions of protein helices. Protein Sci 1997;6:1333-1337.
    • (1997) Protein Sci , vol.6 , pp. 1333-1337
    • Dahiyat, B.I.1    Gordon, D.B.2    Mayo, S.L.3
  • 90
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Dong X, Tsai C-J, Nussinov R. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng 1997;10:999-1012.
    • (1997) Protein Eng , vol.10 , pp. 999-1012
    • Dong, X.1    Tsai, C.-J.2    Nussinov, R.3
  • 91
    • 0018800867 scopus 로고
    • Dynamic information from protein crystallography. An analysis of temperature factors from refinement of the hen egg-white lysozyme structure
    • Sternberg MJ, Grace DE, Phillips DC. Dynamic information from protein crystallography. An analysis of temperature factors from refinement of the hen egg-white lysozyme structure. J Mol Biol 1979;130:231-252.
    • (1979) J Mol Biol , vol.130 , pp. 231-252
    • Sternberg, M.J.1    Grace, D.E.2    Phillips, D.C.3
  • 92
    • 0026641163 scopus 로고
    • Thermodynamics of protein-peptide interactions in the ribonuclease-S system studied by molecular dynamics and free energy calculations
    • Simonson T, Brunger AT. Thermodynamics of protein-peptide interactions in the ribonuclease-S system studied by molecular dynamics and free energy calculations. Biochemistry 1992;31:8661-8674.
    • (1992) Biochemistry , vol.31 , pp. 8661-8674
    • Simonson, T.1    Brunger, A.T.2
  • 93
    • 0030984117 scopus 로고    scopus 로고
    • Variations on a theme by Debye and Waller: From simple crystals to proteins
    • Garcia AE, Krumhansl JA, Frauenfelder H. Variations on a theme by Debye and Waller: from simple crystals to proteins. Proteins 1997;29:153-160.
    • (1997) Proteins , vol.29 , pp. 153-160
    • Garcia, A.E.1    Krumhansl, J.A.2    Frauenfelder, H.3
  • 94
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic Ras proteins
    • Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic Ras proteins. Science 1990;247:939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    DeVos, A.M.3    Brunger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 96
    • 0347602124 scopus 로고    scopus 로고
    • Converging free energy estimates: MM-PB(GB)SA studies on the protein-protein complex Ras-Raf
    • Gohlke H, Case DA. Converging free energy estimates: MM-PB(GB)SA studies on the protein-protein complex Ras-Raf. J Comput Chem 2004;25:238-250.
    • (2004) J Comput Chem , vol.25 , pp. 238-250
    • Gohlke, H.1    Case, D.A.2
  • 97
    • 0034622725 scopus 로고    scopus 로고
    • Identifying the adaptive mechanism in globular proteins: Fluctuations in densely packed regions manipulate flexible parts
    • Yilmaz LS, Atilgan AR. Identifying the adaptive mechanism in globular proteins: fluctuations in densely packed regions manipulate flexible parts. J Chem Phys 2000;113:4454-4464.
    • (2000) J Chem Phys , vol.113 , pp. 4454-4464
    • Yilmaz, L.S.1    Atilgan, A.R.2
  • 98
    • 0035342460 scopus 로고    scopus 로고
    • Elucidating the structural mechanisms for biological activity of the chemokyne family
    • Baysal C, Atilgan AR. Elucidating the structural mechanisms for biological activity of the chemokyne family. Proteins 2001;43:150-160.
    • (2001) Proteins , vol.43 , pp. 150-160
    • Baysal, C.1    Atilgan, A.R.2
  • 99
    • 0033621118 scopus 로고    scopus 로고
    • The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme
    • Freire E. The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme. Proc Natl Acad Sci USA 1999;96:10118-10122.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10118-10122
    • Freire, E.1
  • 100
    • 0030221148 scopus 로고    scopus 로고
    • Interactions between Ras proteins and their effectors
    • McCormick F, Wittinghofer A. Interactions between Ras proteins and their effectors. Curr Opin Biotech 1996;7:449-456.
    • (1996) Curr Opin Biotech , vol.7 , pp. 449-456
    • McCormick, F.1    Wittinghofer, A.2
  • 101
    • 0035087327 scopus 로고    scopus 로고
    • Regulation of the Raf kinase by phosphorylation
    • Zhang B-H, Guan K-L. Regulation of the Raf kinase by phosphorylation. Exp Lung Res 2001;27:269-295.
    • (2001) Exp Lung Res , vol.27 , pp. 269-295
    • Zhang, B.-H.1    Guan, K.-L.2
  • 102
    • 0034874258 scopus 로고    scopus 로고
    • Molecular dynamics force probe simulations of antibody/antigen unbinding: Entropic control and nonadditivity of unbinding forces
    • Heymann B, Grubmuller H. Molecular dynamics force probe simulations of antibody/antigen unbinding: entropic control and nonadditivity of unbinding forces. Biophys J 2001;81:1295-1313.
    • (2001) Biophys J , vol.81 , pp. 1295-1313
    • Heymann, B.1    Grubmuller, H.2
  • 103
    • 0029968247 scopus 로고    scopus 로고
    • Global changes in amide hydrogen exchange rates for a protein antigen in complex with three different antibodies
    • Williams DC, Jr., Benjamin DC, Poljak RJ, Rule GS. Global changes in amide hydrogen exchange rates for a protein antigen in complex with three different antibodies. J Mol Biol 1996;257:866-876.
    • (1996) J Mol Biol , vol.257 , pp. 866-876
    • Williams Jr., D.C.1    Benjamin, D.C.2    Poljak, R.J.3    Rule, G.S.4
  • 104
    • 0000496772 scopus 로고    scopus 로고
    • Vibrational dynamics of folded proteins: Significance of slow and fast modes in relation to function and stability
    • Bahar I, Atilgan AR, Demirel MC, Erman B. Vibrational dynamics of folded proteins: Significance of slow and fast modes in relation to function and stability. Phys Rev Lett 1998;80:2733-2736.
    • (1998) Phys Rev Lett , vol.80 , pp. 2733-2736
    • Bahar, I.1    Atilgan, A.R.2    Demirel, M.C.3    Erman, B.4
  • 105
    • 0021658956 scopus 로고
    • Allostery without conformational change. A plausible model
    • Cooper A, Dryden DT. Allostery without conformational change. A plausible model. Eur Biophys J 1984;11:103-109.
    • (1984) Eur Biophys J , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.2


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