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Volumn 5, Issue 3, 2009, Pages

Ras conformational switching: Simulating nucleotide- dependent conformational transitions with accelerated molecular dynamics

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROLIFERATION; CELL SIGNALING; MOLECULAR DYNAMICS; REACTION INTERMEDIATES; REACTION KINETICS;

EID: 63549096871     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000325     Document Type: Article
Times cited : (159)

References (33)
  • 3
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter IR, Wittinghofer A (2001) The guanine nucleotide-binding switch in three dimensions. Science 294: 1299-1304.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 4
    • 0029107760 scopus 로고
    • The 2.2 A 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, et al. (1995) The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 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
  • 5
    • 21844465952 scopus 로고    scopus 로고
    • Structure of the G60A mutant of Ras: Implications for the dominant negative effect
    • Ford B, Skowronek K, Boykevisch S, Bar-Sagi D, Nassar N (2005) Structure of the G60A mutant of Ras: implications for the dominant negative effect. J Biol Chem 280: 25697-25705.
    • (2005) J Biol Chem , vol.280 , pp. 25697-25705
    • Ford, B.1    Skowronek, K.2    Boykevisch, S.3    Bar-Sagi, D.4    Nassar, N.5
  • 6
    • 0037125971 scopus 로고    scopus 로고
    • The structural basis for the transition from Ras-GTP to Ras-GDP
    • Hall BE, Bar-Sagi D, Nassar N (2002) The structural basis for the transition from Ras-GTP to Ras-GDP. Proc Natl Acad Sci U S A 99: 12138-12142.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12138-12142
    • Hall, B.E.1    Bar-Sagi, D.2    Nassar, N.3
  • 7
    • 33644835005 scopus 로고    scopus 로고
    • Structure of a transient intermediate for GTP hydrolysis by ras
    • Ford B, Hornak V, Kleinman H, Nassar N (2006) Structure of a transient intermediate for GTP hydrolysis by ras. Structure 14: 427-436.
    • (2006) Structure , vol.14 , pp. 427-436
    • Ford, B.1    Hornak, V.2    Kleinman, H.3    Nassar, N.4
  • 8
    • 33746326517 scopus 로고    scopus 로고
    • Structure-function based design of small molecule inhibitors targeting Rho family GTPases
    • Nassar N, Cancelas J, Zheng J, Williams DA, Zheng Y (2006) Structure-function based design of small molecule inhibitors targeting Rho family GTPases. Curr Top Med Chem 6: 1109-1116.
    • (2006) Curr Top Med Chem , vol.6 , pp. 1109-1116
    • Nassar, N.1    Cancelas, J.2    Zheng, J.3    Williams, D.A.4    Zheng, Y.5
  • 9
    • 0035916283 scopus 로고    scopus 로고
    • Structure of the metal-water complex in Ras6GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy
    • Rohrer M, Prisner TF, Brugmann O, Kass H, Spoerner M, et al. (2001) Structure of the metal-water complex in Ras6GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy. Biochemistry 40: 1884-1889.
    • (2001) Biochemistry , vol.40 , pp. 1884-1889
    • Rohrer, M.1    Prisner, T.F.2    Brugmann, O.3    Kass, H.4    Spoerner, M.5
  • 11
    • 0029156702 scopus 로고
    • Molecular dynamics simulation of the solution structures of Ha-ras-p21 GDP and GTP complexes: Flexibility, possible hinges, and levers of the conformational transition
    • Diaz JF, Wroblowski B, Engelborghs Y (1995) Molecular dynamics simulation of the solution structures of Ha-ras-p21 GDP and GTP complexes: flexibility, possible hinges, and levers of the conformational transition. Biochemistry 34: 12038-12047.
    • (1995) Biochemistry , vol.34 , pp. 12038-12047
    • Diaz, J.F.1    Wroblowski, B.2    Engelborghs, Y.3
  • 13
    • 0030711616 scopus 로고    scopus 로고
    • Molecular switch in signal transduction: Reaction paths of the conformational changes in ras p21
    • Ma J, Karplus M (1997) Molecular switch in signal transduction: reaction paths of the conformational changes in ras p21. Proc Natl Acad Sci U S A 94: 11905-11910.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11905-11910
    • Ma, J.1    Karplus, M.2
  • 14
    • 0242618314 scopus 로고    scopus 로고
    • Calculation of pathways for the conformational transition between the GTP- and GDP-bound states of the Ha-ras-p21 protein: Calculations with explicit solvent simulations and comparison with calculations in vacuum
    • Diaz JF, Wroblowski B, Schlitter J, Engelborghs Y (1997) Calculation of pathways for the conformational transition between the GTP- and GDP-bound states of the Ha-ras-p21 protein: calculations with explicit solvent simulations and comparison with calculations in vacuum. Proteins 28: 434-451.
    • (1997) Proteins , vol.28 , pp. 434-451
    • Diaz, J.F.1    Wroblowski, B.2    Schlitter, J.3    Engelborghs, Y.4
  • 15
  • 16
    • 63549092460 scopus 로고    scopus 로고
    • Mapping the nucleotide and isoform dependent structural and dynamical features of Ras proteins
    • Gorfe AA, Grant BJ, McCammon JA (2008) Mapping the nucleotide and isoform dependent structural and dynamical features of Ras proteins. Structure 27: 727-735.
    • (2008) Structure , vol.27 , pp. 727-735
    • Gorfe, A.A.1    Grant, B.J.2    McCammon, J.A.3
  • 17
    • 38449096891 scopus 로고    scopus 로고
    • Sampling of slow diffusive conformational transitions with accelerated molecular dynamics
    • Hamelberg D, de Oliveira CA, McCammon JA (2007) Sampling of slow diffusive conformational transitions with accelerated molecular dynamics. J Chem Phys 127: 155102.
    • (2007) J Chem Phys , vol.127 , pp. 155102
    • Hamelberg, D.1    de Oliveira, C.A.2    McCammon, J.A.3
  • 18
    • 3142716857 scopus 로고    scopus 로고
    • Accelerated molecular dynamics: A promising and efficient simulation method for biomolecules
    • Hamelberg D, Mongan J, McCammon JA (2004) Accelerated molecular dynamics: a promising and efficient simulation method for biomolecules. J Chem Phys 120: 11919-11929.
    • (2004) J Chem Phys , vol.120 , pp. 11919-11929
    • Hamelberg, D.1    Mongan, J.2    McCammon, J.A.3
  • 19
    • 0035067187 scopus 로고    scopus 로고
    • GTP-dependent segregation of H-ras from lipid rafts is required for biological activity
    • Prior IA, Harding A, Yan J, Sluimer J, Parton RG, et al. (2001) GTP-dependent segregation of H-ras from lipid rafts is required for biological activity. Nat Cell Biol 3: 368-375.
    • (2001) Nat Cell Biol , vol.3 , pp. 368-375
    • Prior, I.A.1    Harding, A.2    Yan, J.3    Sluimer, J.4    Parton, R.G.5
  • 20
    • 22144479017 scopus 로고    scopus 로고
    • Ras plasma membrane signalling platforms
    • Hancock JF, Parton RG (2005) Ras plasma membrane signalling platforms. Biochem J 389: 1-11.
    • (2005) Biochem J , vol.389 , pp. 1-11
    • Hancock, J.F.1    Parton, R.G.2
  • 21
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • Plowman SJ, Muncke C, Parton RG, Hancock JF (2005) H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc Natl Acad Sci U S A 102: 15500-15505.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 22
    • 40949130399 scopus 로고    scopus 로고
    • A novel switch region regulates H-ras membrane orientation and signal output
    • Abankwa D, Hanzal-Bayer M, Ariotti N, Plowman SJ, Gorfe AA, et al. (2008) A novel switch region regulates H-ras membrane orientation and signal output. EMBO J 27: 727-735.
    • (2008) EMBO J , vol.27 , pp. 727-735
    • Abankwa, D.1    Hanzal-Bayer, M.2    Ariotti, N.3    Plowman, S.J.4    Gorfe, A.A.5
  • 23
    • 33847413103 scopus 로고    scopus 로고
    • Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2- dimyristoylglycero-3-phosphocholine bilayer
    • Gorfe AA, Hanzal-Bayer M, Abankwa D, Hancock JF, McCammon JA (2007) Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2- dimyristoylglycero-3-phosphocholine bilayer. J Med Chem 50: 674-684.
    • (2007) J Med Chem , vol.50 , pp. 674-684
    • Gorfe, A.A.1    Hanzal-Bayer, M.2    Abankwa, D.3    Hancock, J.F.4    McCammon, J.A.5
  • 24
    • 33646742004 scopus 로고    scopus 로고
    • Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations
    • Zheng W, Brooks BR, Thirumalai D (2006) Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations. Proc Natl Acad Sci U S A 103: 7664-7669.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7664-7669
    • Zheng, W.1    Brooks, B.R.2    Thirumalai, D.3
  • 25
    • 0034308140 scopus 로고    scopus 로고
    • Building-block approach for determining low-frequency normal modes of macromolecules
    • Tama F, Gadea FX, Marques O, Sanejouand YH (2000) Building-block approach for determining low-frequency normal modes of macromolecules. Proteins 41: 1-7.
    • (2000) Proteins , vol.41 , pp. 1-7
    • Tama, F.1    Gadea, F.X.2    Marques, O.3    Sanejouand, Y.H.4
  • 26
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama F, Sanejouand YH (2001) Conformational change of proteins arising from normal mode calculations. Protein Eng 14: 1-6.
    • (2001) Protein Eng , vol.14 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.H.2
  • 28
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, et al. (2006) Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 65: 712-725.
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5
  • 29
    • 0037495965 scopus 로고    scopus 로고
    • Development of polyphosphate parameters for use with the AMBER force field
    • Meagher KL, Redman LT, Carlson HA (2003) Development of polyphosphate parameters for use with the AMBER force field. J Comput Chem 24: 1016-1025.
    • (2003) J Comput Chem , vol.24 , pp. 1016-1025
    • Meagher, K.L.1    Redman, L.T.2    Carlson, H.A.3
  • 31
    • 34247237308 scopus 로고    scopus 로고
    • Multivariate analysis of conserved sequence-structure relationships in kinesins: Coupling of the active site and a tubulin-binding sub-domain
    • Grant BJ, McCammon JA, Caves LS, Cross RA (2007) Multivariate analysis of conserved sequence-structure relationships in kinesins: coupling of the active site and a tubulin-binding sub-domain. J Mol Biol 368: 1231-1248.
    • (2007) J Mol Biol , vol.368 , pp. 1231-1248
    • Grant, B.J.1    McCammon, J.A.2    Caves, L.S.3    Cross, R.A.4
  • 33
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye T, Karplus M (1991) Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins 11: 205-217.
    • (1991) Proteins , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2


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