메뉴 건너뛰기




Volumn 189, Issue , 2014, Pages 33-39

Distinguishing induced fit from conformational selection

Author keywords

Conformational selection; Induced fit; Kinetics; Protein protein interactions

Indexed keywords

LIGAND; PROTEIN;

EID: 84898953700     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2014.03.003     Document Type: Article
Times cited : (133)

References (42)
  • 1
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • D.E. Koshland Application of a theory of enzyme specificity to protein synthesis Proc. Natl. Acad. Sci. U. S. A. 44 1958 98 104
    • (1958) Proc. Natl. Acad. Sci. U. S. A. , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 2
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • J. Monod, J. Wyman, and J.P. Changeux On the nature of allosteric transitions: a plausible model J. Mol. Biol. 12 1965 88 118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 3
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • D.E. Koshland Jr., G. Némethy, and D. Filmer Comparison of experimental binding data and theoretical models in proteins containing subunits Biochemistry 5 1966 365 385
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, Jr.D.E.1    Némethy, G.2    Filmer, D.3
  • 5
    • 42949129270 scopus 로고    scopus 로고
    • A Coupled Equilibrium Shift Mechanism in Calmodulin-Mediated Signal Transduction
    • DOI 10.1016/j.str.2008.02.017, PII S0969212608001317
    • J. Gsponer, J. Christodoulou, A. Cavalli, J.M. Bui, B. Richter, and C.M. Dobson et al. A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction Structure 1993 16 2008 736 746 10.1016/j.str.2008.02.017 (Pubitemid 351615020)
    • (2008) Structure , vol.16 , Issue.5 , pp. 736-746
    • Gsponer, J.1    Christodoulou, J.2    Cavalli, A.3    Bui, J.M.4    Richter, B.5    Dobson, C.M.6    Vendruscolo, M.7
  • 6
    • 80053539881 scopus 로고    scopus 로고
    • Conformational selection or induced fit? 50 years of debate resolved, F1000
    • 10.3410/B3-19
    • J.-P. Changeux, and S. Edelstein Conformational selection or induced fit? 50 years of debate resolved, F1000 Biol. Rep. 3 2011 19 10.3410/B3-19
    • (2011) Biol. Rep. , vol.3 , pp. 19
    • Changeux, J.-P.1    Edelstein, S.2
  • 9
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • 10.1110/ps.03259908
    • Q. Cui, and M. Karplus Allostery and cooperativity revisited Protein Sci. Publ. Protein Soc. 17 2008 1295 1307 10.1110/ps.03259908
    • (2008) Protein Sci. Publ. Protein Soc. , vol.17 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 10
    • 84857839467 scopus 로고    scopus 로고
    • Multiparametric analysis of intrinsically disordered proteins: Looking at intrinsic disorder through compound eyes
    • 10.1021/ac203096k
    • V.N. Uversky, and A.K. Dunker Multiparametric analysis of intrinsically disordered proteins: looking at intrinsic disorder through compound eyes Anal. Chem. 84 2012 2096 2104 10.1021/ac203096k
    • (2012) Anal. Chem. , vol.84 , pp. 2096-2104
    • Uversky, V.N.1    Dunker, A.K.2
  • 11
    • 84856708599 scopus 로고    scopus 로고
    • Intrinsic disorder: Signaling via highly specific but short-lived association
    • 10.1016/j.tibs.2011.11.002
    • H.-X. Zhou Intrinsic disorder: signaling via highly specific but short-lived association Trends Biochem. Sci. 37 2012 43 48 10.1016/j.tibs.2011. 11.002
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 43-48
    • Zhou, H.-X.1
  • 12
    • 84896336036 scopus 로고    scopus 로고
    • The binding mechanisms of intrinsically disordered proteins
    • 10.1039/c3cp54226b
    • J. Dogan, S. Gianni, and P. Jemth The binding mechanisms of intrinsically disordered proteins Phys. Chem. Chem. Phys. PCCP. 16 2014 6323 6331 10.1039/c3cp54226b
    • (2014) Phys. Chem. Chem. Phys. PCCP. , vol.16 , pp. 6323-6331
    • Dogan, J.1    Gianni, S.2    Jemth, P.3
  • 13
    • 84864462749 scopus 로고    scopus 로고
    • Conformational selection or induced fit? A critical appraisal of the kinetic mechanism
    • 10.1021/bi3006913
    • A.D. Vogt, and E. Di Cera Conformational selection or induced fit? A critical appraisal of the kinetic mechanism Biochemistry 51 2012 5894 5902 10.1021/bi3006913
    • (2012) Biochemistry , vol.51 , pp. 5894-5902
    • Vogt, A.D.1    Di Cera, E.2
  • 14
    • 84883213263 scopus 로고    scopus 로고
    • Conformational selection is a dominant mechanism of ligand binding
    • 10.1021/bi400929b
    • A.D. Vogt, and E. Di Cera Conformational selection is a dominant mechanism of ligand binding Biochemistry 52 2013 5723 5729 10.1021/bi400929b
    • (2013) Biochemistry , vol.52 , pp. 5723-5729
    • Vogt, A.D.1    Di Cera, E.2
  • 15
    • 84894262099 scopus 로고    scopus 로고
    • Essential role of conformational selection in ligand binding
    • 10.1016/j.bpc.2013.09.003
    • A.D. Vogt, N. Pozzi, Z. Chen, and E. Di Cera Essential role of conformational selection in ligand binding Biophys. Chem. 186C 2014 13 21 10.1016/j.bpc.2013.09.003
    • (2014) Biophys. Chem. , vol.186 C , pp. 13-21
    • Vogt, A.D.1    Pozzi, N.2    Chen, Z.3    Di Cera, E.4
  • 16
    • 0001195192 scopus 로고
    • The binding of nicotinamide-adenine dinucleotide to yeast d-glyceraldehyde-3-phosphate dehydrogenase: Temperature-jump relaxation studies on the mechanism of an allosteric enzyme
    • K. Kirschner, M. Eigen, R. Bittman, and B. Voigt The binding of nicotinamide-adenine dinucleotide to yeast d-glyceraldehyde-3-phosphate dehydrogenase: temperature-jump relaxation studies on the mechanism of an allosteric enzyme Proc. Natl. Acad. Sci. U. S. A. 56 1966 1661 1667
    • (1966) Proc. Natl. Acad. Sci. U. S. A. , vol.56 , pp. 1661-1667
    • Kirschner, K.1    Eigen, M.2    Bittman, R.3    Voigt, B.4
  • 17
    • 0026033193 scopus 로고
    • Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant
    • S.S. Patel, I. Wong, and K.A. Johnson Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant Biochemistry 30 1991 511 525
    • (1991) Biochemistry , vol.30 , pp. 511-525
    • Patel, S.S.1    Wong, I.2    Johnson, K.A.3
  • 18
    • 0026026192 scopus 로고
    • An induced-fit kinetic mechanism for DNA replication fidelity: Direct measurement by single-turnover kinetics
    • I. Wong, S.S. Patel, and K.A. Johnson An induced-fit kinetic mechanism for DNA replication fidelity: direct measurement by single-turnover kinetics Biochemistry 30 1991 526 537
    • (1991) Biochemistry , vol.30 , pp. 526-537
    • Wong, I.1    Patel, S.S.2    Johnson, K.A.3
  • 19
    • 55549109430 scopus 로고    scopus 로고
    • Role of induced fit in enzyme specificity: A molecular forward/reverse switch
    • 10.1074/jbc.R800034200
    • K.A. Johnson Role of induced fit in enzyme specificity: a molecular forward/reverse switch J. Biol. Chem. 283 2008 26297 26301 10.1074/jbc. R800034200
    • (2008) J. Biol. Chem. , vol.283 , pp. 26297-26301
    • Johnson, K.A.1
  • 20
    • 0015152607 scopus 로고
    • Escherichia coli alkaline phosphatase. An analysis of transient kinetics
    • S.E. Halford Escherichia coli alkaline phosphatase. An analysis of transient kinetics Biochem. J. 125 1971 319 327
    • (1971) Biochem. J. , vol.125 , pp. 319-327
    • Halford, S.E.1
  • 21
    • 0019821957 scopus 로고
    • Binding of high affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction
    • S.T. Olson, K.R. Srinivasan, I. Björk, and J.D. Shore Binding of high affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction J. Biol. Chem. 256 1981 11073 11079 (Pubitemid 12181591)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.21 , pp. 11073-11079
    • Olson, S.T.1    Srinivasan, K.R.2    Bjork, I.3    Shore, J.D.4
  • 22
    • 0037118717 scopus 로고    scopus 로고
    • Kinetics of the E. Coli replication factor DnaC protein-nucleotide interactions. II. Fluorescence anisotropy and transient, dynamic quenching stopped-flow studies of the reaction intermediatest
    • DOI 10.1021/bi020127w
    • R. Galletto, and W. Bujalowski Kinetics of the E. coli replication factor DnaC protein-nucleotide interactions. II. Fluorescence anisotropy and transient, dynamic quenching stopped-flow studies of the reaction intermediates Biochemistry 41 2002 8921 8934 (Pubitemid 34774405)
    • (2002) Biochemistry , vol.41 , Issue.28 , pp. 8921-8934
    • Galletto, R.1    Bujalowski, W.2
  • 23
    • 24044468582 scopus 로고    scopus 로고
    • Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: Analysis of stopped-flow kinetic experiments
    • DOI 10.1385/CBB:42:2:121
    • R. Galletto, M.J. Jezewska, and W. Bujalowski Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: analysis of stopped-flow kinetic experiments Cell Biochem. Biophys. 42 2005 121 144 10.1385/CBB:42:2:121 (Pubitemid 41270735)
    • (2005) Cell Biochemistry and Biophysics , vol.42 , Issue.2 , pp. 121-144
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 24
    • 13444306219 scopus 로고    scopus 로고
    • Kinetic mechanism of rat polymerase β-dsDNA interactions. Fluorescence stopped-flow analysis of the cooperative ligand binding to a two-site one-dimensional lattice
    • DOI 10.1021/bi0487037
    • R. Galletto, M.J. Jezewska, and W. Bujalowski Kinetic mechanism of rat polymerase beta-dsDNA interactions. Fluorescence stopped-flow analysis of the cooperative ligand binding to a two-site one-dimensional lattice Biochemistry 44 2005 1251 1267 10.1021/bi0487037 (Pubitemid 40209005)
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1251-1267
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 27
    • 21844437963 scopus 로고    scopus 로고
    • The study of bimolecular reactions under non-pseudo-first order conditions
    • DOI 10.1016/j.bpc.2005.04.006, PII S0301462205000864
    • F. Malatesta The study of bimolecular reactions under non-pseudo-first order conditions Biophys. Chem. 116 2005 251 256 10.1016/j.bpc.2005.04.006 (Pubitemid 40962453)
    • (2005) Biophysical Chemistry , vol.116 , Issue.3 , pp. 251-256
    • Malatesta, F.1
  • 28
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental aspects of protein-protein association kinetics
    • 10.1021/cr800373w
    • G. Schreiber, G. Haran, and H.-X. Zhou Fundamental aspects of protein-protein association kinetics Chem. Rev. 109 2009 839 860 10.1021/cr800373w
    • (2009) Chem. Rev. , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.-X.3
  • 29
    • 0015298504 scopus 로고
    • Escherichia coli alkaline phosphatase. Relaxation spectra of ligand binding
    • S.E. Halford Escherichia coli alkaline phosphatase. Relaxation spectra of ligand binding Biochem. J. 126 1972 727 738
    • (1972) Biochem. J. , vol.126 , pp. 727-738
    • Halford, S.E.1
  • 30
    • 0028903531 scopus 로고
    • Transient kinetic approaches to enzyme mechanisms
    • C.A. Fierke, and G.G. Hammes Transient kinetic approaches to enzyme mechanisms Methods Enzymol. 249 1995 3 37
    • (1995) Methods Enzymol. , vol.249 , pp. 3-37
    • Fierke, C.A.1    Hammes, G.G.2
  • 31
    • 78149358266 scopus 로고    scopus 로고
    • Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors
    • S.T. Olson, B. Richard, G. Izaguirre, S. Schedin-Weiss, and P.G.W. Gettins Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors Biochimie 92 2010 1587 1596
    • (2010) Biochimie , vol.92 , pp. 1587-1596
    • Olson, S.T.1    Richard, B.2    Izaguirre, G.3    Schedin-Weiss, S.4    Gettins, P.G.W.5
  • 33
    • 84884245462 scopus 로고    scopus 로고
    • Structures and target recognition modes of PDZ domains: Recurring themes and emerging pictures
    • 10.1042/BJ20130783
    • F. Ye, and M. Zhang Structures and target recognition modes of PDZ domains: recurring themes and emerging pictures Biochem. J. 455 2013 1 14 10.1042/BJ20130783
    • (2013) Biochem. J. , vol.455 , pp. 1-14
    • Ye, F.1    Zhang, M.2
  • 34
    • 84864615365 scopus 로고    scopus 로고
    • Plasticity of PDZ domains in ligand recognition and signaling
    • 10.1016/j.febslet.2012.04.015
    • Y. Ivarsson Plasticity of PDZ domains in ligand recognition and signaling FEBS Lett. 586 2012 2638 2647 10.1016/j.febslet.2012.04.015
    • (2012) FEBS Lett. , vol.586 , pp. 2638-2647
    • Ivarsson, Y.1
  • 36
    • 1642276423 scopus 로고    scopus 로고
    • Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition
    • DOI 10.1016/S1097-2765(04)00086-3, PII S1097276504000863
    • F.C. Peterson, R.R. Penkert, B.F. Volkman, and K.E. Prehoda Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition Mol. Cell 13 2004 665 676 (Pubitemid 38368124)
    • (2004) Molecular Cell , vol.13 , Issue.5 , pp. 665-676
    • Peterson, F.C.1    Penkert, R.R.2    Volkman, B.F.3    Prehoda, K.E.4
  • 38
    • 84867280715 scopus 로고    scopus 로고
    • Fast association and slow transitions in the interaction between two intrinsically disordered protein domains
    • 10.1074/jbc.M112.399436
    • J. Dogan, T. Schmidt, X. Mu, Å. Engström, and P. Jemth Fast association and slow transitions in the interaction between two intrinsically disordered protein domains J. Biol. Chem. 287 2012 34316 34324 10.1074/jbc.M112.399436
    • (2012) J. Biol. Chem. , vol.287 , pp. 34316-34324
    • Dogan, J.1    Schmidt, T.2    Mu, X.3    Engström, Å.4    Jemth, P.5
  • 39
    • 0031969090 scopus 로고    scopus 로고
    • A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale
    • M.C. Shastry, S.D. Luck, and H. Roder A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale Biophys. J. 74 1998 2714 2721 10.1016/S0006-3495(98)77977-9 (Pubitemid 28225265)
    • (1998) Biophysical Journal , vol.74 , Issue.5 , pp. 2714-2721
    • Shastry, M.C.R.1    Luck, S.D.2    Roder, H.3
  • 41
    • 0037203771 scopus 로고    scopus 로고
    • Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
    • DOI 10.1038/415549a
    • S.J. Demarest, M. Martinez-Yamout, J. Chung, H. Chen, W. Xu, and H.J. Dyson et al. Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators Nature 415 2002 549 553 10.1038/415549a (Pubitemid 34130612)
    • (2002) Nature , vol.415 , Issue.6871 , pp. 549-553
    • Demarest, S.J.1    Martinez-Yamout, M.2    Chung, J.3    Chen, H.4    Xu, W.5    Jane Dyson, H.6    Evans, R.M.7    Wright, P.E.8
  • 42
    • 0003845223 scopus 로고    scopus 로고
    • The PyMol Molecular Graphics System
    • W.L. DeLano The PyMol Molecular Graphics System Schrödinger 2002 http://www.pymol.org
    • (2002) Schrödinger
    • Delano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.