메뉴 건너뛰기




Volumn 14, Issue 1, 2016, Pages 32-42

Conformational Selection in a Protein-Protein Interaction Revealed by Dynamic Pathway Analysis

Author keywords

Conformational ensemble; Conformational selection; Energy landscape; Molecular recognition dynamics; Protein protein interaction; Recoverin

Indexed keywords

RECOVERIN; RHODOPSIN KINASE; PROTEIN BINDING; RCVRN PROTEIN, HUMAN;

EID: 84952978925     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2015.12.010     Document Type: Article
Times cited : (53)

References (73)
  • 1
    • 84923367313 scopus 로고    scopus 로고
    • Energetic dissection of Gleevec's selectivity toward human tyrosine kinases
    • Agafonov R.V., Wilson C., Otten R., Buosi V., Kern D. Energetic dissection of Gleevec's selectivity toward human tyrosine kinases. Nat. Struct. Mol. Biol. 2014, 21:848-853.
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 848-853
    • Agafonov, R.V.1    Wilson, C.2    Otten, R.3    Buosi, V.4    Kern, D.5
  • 2
    • 84890117217 scopus 로고    scopus 로고
    • NMR studies of nucleic acid dynamics
    • Al-Hashimi H.M. NMR studies of nucleic acid dynamics. J. Magn. Reson. 2013, 237:191-204.
    • (2013) J. Magn. Reson. , vol.237 , pp. 191-204
    • Al-Hashimi, H.M.1
  • 3
    • 0028037860 scopus 로고
    • Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch
    • Ames J.B., Tanaka T., Stryer L., Ikura M. Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch. Biochemistry 1994, 33:10743-10753.
    • (1994) Biochemistry , vol.33 , pp. 10743-10753
    • Ames, J.B.1    Tanaka, T.2    Stryer, L.3    Ikura, M.4
  • 4
    • 0029564421 scopus 로고
    • Nuclear magnetic resonance evidence for Ca(2+)-induced extrusion of the myristoyl group of recoverin
    • Ames J.B., Tanaka T., Ikura M., Stryer L. Nuclear magnetic resonance evidence for Ca(2+)-induced extrusion of the myristoyl group of recoverin. J. Biol. Chem. 1995, 270:30909-30913.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30909-30913
    • Ames, J.B.1    Tanaka, T.2    Ikura, M.3    Stryer, L.4
  • 6
    • 33846010489 scopus 로고    scopus 로고
    • Structural basis for calcium-induced inhibition of rhodopsin kinase by recoverin
    • Ames J.B., Levay K., Wingard J.N., Lusin J.D., Slepak V.Z. Structural basis for calcium-induced inhibition of rhodopsin kinase by recoverin. J. Biol. Chem. 2006, 281:37237-37245.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37237-37245
    • Ames, J.B.1    Levay, K.2    Wingard, J.N.3    Lusin, J.D.4    Slepak, V.Z.5
  • 7
    • 0031547981 scopus 로고    scopus 로고
    • Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase
    • Baker B.M., Murphy K.P. Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase. J. Mol. Biol. 1997, 268:557-569.
    • (1997) J. Mol. Biol. , vol.268 , pp. 557-569
    • Baker, B.M.1    Murphy, K.P.2
  • 8
    • 50149104140 scopus 로고    scopus 로고
    • Interactions between the three CIN85 SH3 domains and ubiquitin: implications for CIN85 ubiquitination
    • Bezsonova I., Bruce M.C., Wiesner S., Lin H., Rotin D., Forman-Kay J.D. Interactions between the three CIN85 SH3 domains and ubiquitin: implications for CIN85 ubiquitination. Biochemistry 2008, 47:8937-8949.
    • (2008) Biochemistry , vol.47 , pp. 8937-8949
    • Bezsonova, I.1    Bruce, M.C.2    Wiesner, S.3    Lin, H.4    Rotin, D.5    Forman-Kay, J.D.6
  • 9
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr D.D., McElheny D., Dyson H.J., Wright P.E. The dynamic energy landscape of dihydrofolate reductase catalysis. Science 2006, 313:1638-1642.
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 10
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr D.D., Nussinov R., Wright P.E. The role of dynamic conformational ensembles in biomolecular recognition. Nat. Chem. Biol. 2009, 5:789-796.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 12
    • 0035156560 scopus 로고    scopus 로고
    • The neuronal calcium sensor family of Ca2+-binding proteins
    • Burgoyne R.D., Weiss J.L. The neuronal calcium sensor family of Ca2+-binding proteins. Biochem. J. 2001, 353:1-12.
    • (2001) Biochem. J. , vol.353 , pp. 1-12
    • Burgoyne, R.D.1    Weiss, J.L.2
  • 13
    • 0002889918 scopus 로고
    • General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation
    • Carver J.P., Richards R.E. General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. J. Magn. Reson. 1972, 6:89-96.
    • (1972) J. Magn. Reson. , vol.6 , pp. 89-96
    • Carver, J.P.1    Richards, R.E.2
  • 15
    • 80053539881 scopus 로고    scopus 로고
    • Conformational selection or induced fit? 50 years of debate resolved
    • Changeux J.P., Edelstein S. Conformational selection or induced fit? 50 years of debate resolved. F1000 Biol. Rep. 2011, 3:19.
    • (2011) F1000 Biol. Rep. , vol.3 , pp. 19
    • Changeux, J.P.1    Edelstein, S.2
  • 16
    • 0028978240 scopus 로고
    • Ca(2+)-dependent interaction of recoverin with rhodopsin kinase
    • Chen C.K., Inglese J., Lefkowitz R.J., Hurley J.B. Ca(2+)-dependent interaction of recoverin with rhodopsin kinase. J. Biol. Chem. 1995, 270:18060-18066.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18060-18066
    • Chen, C.K.1    Inglese, J.2    Lefkowitz, R.J.3    Hurley, J.B.4
  • 17
    • 84894280807 scopus 로고    scopus 로고
    • Interplay between conformational selection and induced fit in multidomain protein-ligand binding probed by paramagnetic relaxation enhancement
    • Clore G.M. Interplay between conformational selection and induced fit in multidomain protein-ligand binding probed by paramagnetic relaxation enhancement. Biophys. Chem. 2014, 186:3-12.
    • (2014) Biophys. Chem. , vol.186 , pp. 3-12
    • Clore, G.M.1
  • 18
    • 80052462704 scopus 로고    scopus 로고
    • Conformational adaptation in drug-target interactions and residence time
    • Copeland R.A. Conformational adaptation in drug-target interactions and residence time. Future Med. Chem. 2011, 3:1491-1501.
    • (2011) Future Med. Chem. , vol.3 , pp. 1491-1501
    • Copeland, R.A.1
  • 19
    • 84892818561 scopus 로고    scopus 로고
    • Understanding allosteric and cooperative interactions in enzymes
    • Cornish-Bowden A. Understanding allosteric and cooperative interactions in enzymes. FEBS J. 2014, 281:621-632.
    • (2014) FEBS J. , vol.281 , pp. 621-632
    • Cornish-Bowden, A.1
  • 21
    • 0141940263 scopus 로고    scopus 로고
    • Thermodynamics of the binding of Thermus aquaticus DNA polymerase to primed-template DNA
    • Datta K., LiCata V.J. Thermodynamics of the binding of Thermus aquaticus DNA polymerase to primed-template DNA. Nucleic Acids Res. 2003, 31:5590-5597.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5590-5597
    • Datta, K.1    LiCata, V.J.2
  • 22
    • 0028472289 scopus 로고
    • Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods
    • Davis D.G., Perlman M.E., London R.E. Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods. J. Magn. Reson. B. 1994, 104:266-275.
    • (1994) J. Magn. Reson. B. , vol.104 , pp. 266-275
    • Davis, D.G.1    Perlman, M.E.2    London, R.E.3
  • 24
    • 84894277106 scopus 로고    scopus 로고
    • Special issue on conformational selection
    • Di Cera E. Special issue on conformational selection. Biophys. Chem. 2014, 186:1-2.
    • (2014) Biophys. Chem. , vol.186 , pp. 1-2
    • Di Cera, E.1
  • 25
    • 84894256162 scopus 로고    scopus 로고
    • Exploring the role of receptor flexibility in structure-based drug discovery
    • Feixas F., Lindert S., Sinko W., McCammon J.A. Exploring the role of receptor flexibility in structure-based drug discovery. Biophys. Chem. 2014, 186:31-45.
    • (2014) Biophys. Chem. , vol.186 , pp. 31-45
    • Feixas, F.1    Lindert, S.2    Sinko, W.3    McCammon, J.A.4
  • 28
    • 0027943261 scopus 로고
    • Conformational isomerism and the diversity of antibodies
    • Foote J., Milstein C. Conformational isomerism and the diversity of antibodies. Proc. Natl. Acad. Sci. USA 1994, 91:10370-10374.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10370-10374
    • Foote, J.1    Milstein, C.2
  • 29
    • 0000013706 scopus 로고
    • An equation of state describing hydrophobic interactions
    • Gill S.J., Wadsö I. An equation of state describing hydrophobic interactions. Proc. Natl. Acad. Sci. USA 1976, 73:2955-2958.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2955-2958
    • Gill, S.J.1    Wadsö, I.2
  • 30
    • 84904291286 scopus 로고    scopus 로고
    • Both protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fit
    • Greives N., Zhou H.X. Both protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fit. Proc. Natl. Acad. Sci. USA 2014, 111:10197-10202.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 10197-10202
    • Greives, N.1    Zhou, H.X.2
  • 31
    • 78149240323 scopus 로고    scopus 로고
    • Improved fitting of solution X-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling
    • Grishaev A., Guo L., Irving T., Bax A. Improved fitting of solution X-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling. J. Am. Chem. Soc. 2010, 132:15484-15486.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15484-15486
    • Grishaev, A.1    Guo, L.2    Irving, T.3    Bax, A.4
  • 32
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: a flux description of reaction mechanism
    • Hammes G.G., Chang Y.C., Oas T.G. Conformational selection or induced fit: a flux description of reaction mechanism. Proc. Natl. Acad. Sci. USA 2009, 106:13737-13741.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.C.2    Oas, T.G.3
  • 33
    • 84894264010 scopus 로고    scopus 로고
    • Single molecule insights on conformational selection and induced fit mechanism
    • Hatzakis N.S. Single molecule insights on conformational selection and induced fit mechanism. Biophys. Chem. 2014, 186:46-54.
    • (2014) Biophys. Chem. , vol.186 , pp. 46-54
    • Hatzakis, N.S.1
  • 34
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman K., Kern D. Dynamic personalities of proteins. Nature 2007, 450:964-972.
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 35
    • 33745815637 scopus 로고    scopus 로고
    • Recoverin binds exclusively to an amphipathic peptide at the N terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase
    • Higgins M.K., Oprian D.D., Schertler G.F. Recoverin binds exclusively to an amphipathic peptide at the N terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase. J. Biol. Chem. 2006, 281:19426-19432.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19426-19432
    • Higgins, M.K.1    Oprian, D.D.2    Schertler, G.F.3
  • 36
    • 24644521419 scopus 로고    scopus 로고
    • Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition
    • James L.C., Tawfik D.S. Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition. Proc. Natl. Acad. Sci. USA 2005, 102:12730-12735.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12730-12735
    • James, L.C.1    Tawfik, D.S.2
  • 37
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James L.C., Roversi P., Tawfik D.S. Antibody multispecificity mediated by conformational diversity. Science 2003, 299:1362-1367.
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 38
    • 0001766423 scopus 로고
    • Chemical exchange and Nmr T2 relaxation- multisite case
    • Jen J. Chemical exchange and Nmr T2 relaxation- multisite case. J. Magn. Reson. 1978, 30:111-128.
    • (1978) J. Magn. Reson. , vol.30 , pp. 111-128
    • Jen, J.1
  • 39
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson B.A. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 2004, 278:313-352.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 40
    • 71549171706 scopus 로고    scopus 로고
    • Fitting enzyme kinetic data with KinTek Global Kinetic Explorer
    • Johnson K.A. Fitting enzyme kinetic data with KinTek Global Kinetic Explorer. Methods Enzymol. 2009, 467:601-626.
    • (2009) Methods Enzymol. , vol.467 , pp. 601-626
    • Johnson, K.A.1
  • 41
    • 60549105802 scopus 로고    scopus 로고
    • Global kinetic explorer: a new computer program for dynamic simulation and fitting of kinetic data
    • Johnson K.A., Simpson Z.B., Blom T. Global kinetic explorer: a new computer program for dynamic simulation and fitting of kinetic data. Anal. Biochem. 2009, 387:20-29.
    • (2009) Anal. Biochem. , vol.387 , pp. 20-29
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 42
    • 0029033531 scopus 로고
    • Inhibition of rhodopsin kinase by recoverin. Further evidence for a negative feedback system in phototransduction
    • Klenchin V.A., Calvert P.D., Bownds M.D. Inhibition of rhodopsin kinase by recoverin. Further evidence for a negative feedback system in phototransduction. J. Biol. Chem. 1995, 270:16147-16152.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16147-16152
    • Klenchin, V.A.1    Calvert, P.D.2    Bownds, M.D.3
  • 44
    • 59149097809 scopus 로고    scopus 로고
    • Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy
    • Korzhnev D.M., Bezsonova I., Lee S., Chalikian T.V., Kay L.E. Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy. J. Mol. Biol. 2009, 386:391-405.
    • (2009) J. Mol. Biol. , vol.386 , pp. 391-405
    • Korzhnev, D.M.1    Bezsonova, I.2    Lee, S.3    Chalikian, T.V.4    Kay, L.E.5
  • 45
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland D.E. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. USA 1958, 44:98-104.
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 47
    • 0001039702 scopus 로고
    • Kinetic evidence for hapten-induced conformational transition in immunoglobin MOPC 460
    • Lancet D., Pecht I. Kinetic evidence for hapten-induced conformational transition in immunoglobin MOPC 460. Proc. Natl. Acad. Sci. USA 1976, 73:3549-3553.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3549-3553
    • Lancet, D.1    Pecht, I.2
  • 49
    • 0033226859 scopus 로고    scopus 로고
    • Transverse-relaxation-optimized (TROSY) gradient-enhanced triple-resonance NMR spectroscopy
    • Loria J.P., Rance M., Palmer A.G. Transverse-relaxation-optimized (TROSY) gradient-enhanced triple-resonance NMR spectroscopy. J. Magn. Reson. 1999, 141:180-184.
    • (1999) J. Magn. Reson. , vol.141 , pp. 180-184
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 50
    • 0032719427 scopus 로고    scopus 로고
    • A TROSY CPMG sequence for characterizing chemical exchange in large proteins
    • Loria J.P., Rance M., Palmer A.G. A TROSY CPMG sequence for characterizing chemical exchange in large proteins. J. Biomol. NMR 1999, 15:151-155.
    • (1999) J. Biomol. NMR , vol.15 , pp. 151-155
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 51
    • 84896293788 scopus 로고    scopus 로고
    • Improved cross validation of a static ubiquitin structure derived from high precision residual dipolar couplings measured in a drug-based liquid crystalline phase
    • Maltsev A.S., Grishaev A., Roche J., Zasloff M., Bax A. Improved cross validation of a static ubiquitin structure derived from high precision residual dipolar couplings measured in a drug-based liquid crystalline phase. J. Am. Chem. Soc. 2014, 136:3752-3755.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 3752-3755
    • Maltsev, A.S.1    Grishaev, A.2    Roche, J.3    Zasloff, M.4    Bax, A.5
  • 52
    • 0035909449 scopus 로고    scopus 로고
    • Thermodynamics of the hydrophobic effect. III. Condensation and aggregation of alkanes, alcohols, and alkylamines
    • Matulis D. Thermodynamics of the hydrophobic effect. III. Condensation and aggregation of alkanes, alcohols, and alkylamines. Biophys. Chem. 2001, 93:67-82.
    • (2001) Biophys. Chem. , vol.93 , pp. 67-82
    • Matulis, D.1
  • 54
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., Changeux J.P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 1965, 12:88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 55
    • 0035819455 scopus 로고    scopus 로고
    • Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme
    • Mulder F.A., Skrynnikov N.R., Hon B., Dahlquist F.W., Kay L.E. Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J. Am. Chem. Soc. 2001, 123:967-975.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 967-975
    • Mulder, F.A.1    Skrynnikov, N.R.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 56
    • 84894246676 scopus 로고    scopus 로고
    • Multiple conformational selection and induced fit events take place in allosteric propagation
    • Nussinov R., Ma B., Tsai C.J. Multiple conformational selection and induced fit events take place in allosteric propagation. Biophys. Chem. 2014, 186:22-30.
    • (2014) Biophys. Chem. , vol.186 , pp. 22-30
    • Nussinov, R.1    Ma, B.2    Tsai, C.J.3
  • 57
    • 0027469860 scopus 로고
    • Identification of the N-terminal region in rhodopsin kinase involved in its interaction with rhodopsin
    • Palczewski K., Buczyłko J., Lebioda L., Crabb J.W., Polans A.S. Identification of the N-terminal region in rhodopsin kinase involved in its interaction with rhodopsin. J. Biol. Chem. 1993, 268:6004-6013.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6004-6013
    • Palczewski, K.1    Buczyłko, J.2    Lebioda, L.3    Crabb, J.W.4    Polans, A.S.5
  • 58
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer A.G. NMR characterization of the dynamics of biomacromolecules. Chem. Rev. 2004, 104:3623-3640.
    • (2004) Chem. Rev. , vol.104 , pp. 3623-3640
    • Palmer, A.G.1
  • 59
    • 84896955793 scopus 로고    scopus 로고
    • Chemical exchange in biomacromolecules: past, present, and future
    • Palmer A.G. Chemical exchange in biomacromolecules: past, present, and future. J. Magn. Reson. 2014, 241:3-17.
    • (2014) J. Magn. Reson. , vol.241 , pp. 3-17
    • Palmer, A.G.1
  • 60
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules
    • Palmer A.G., Kroenke C.D., Loria J.P. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 2001, 339:204-238.
    • (2001) Methods Enzymol. , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 62
    • 84890332497 scopus 로고    scopus 로고
    • A highly conserved cysteine of neuronal calcium-sensing proteins controls cooperative binding of Ca2+ to recoverin
    • Ranaghan M.J., Kumar R.P., Chakrabarti K.S., Buosi V., Kern D., Oprian D.D. A highly conserved cysteine of neuronal calcium-sensing proteins controls cooperative binding of Ca2+ to recoverin. J. Biol. Chem. 2013, 288:36160-36167.
    • (2013) J. Biol. Chem. , vol.288 , pp. 36160-36167
    • Ranaghan, M.J.1    Kumar, R.P.2    Chakrabarti, K.S.3    Buosi, V.4    Kern, D.5    Oprian, D.D.6
  • 63
    • 46649109793 scopus 로고    scopus 로고
    • Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation
    • Singh P., Wang B., Maeda T., Palczewski K., Tesmer J.J. Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation. J. Biol. Chem. 2008, 283:14053-14062.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14053-14062
    • Singh, P.1    Wang, B.2    Maeda, T.3    Palczewski, K.4    Tesmer, J.J.5
  • 64
    • 0037120879 scopus 로고    scopus 로고
    • Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments
    • Skrynnikov N.R., Dahlquist F.W., Kay L.E. Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments. J. Am. Chem. Soc. 2002, 124:12352-12360.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12352-12360
    • Skrynnikov, N.R.1    Dahlquist, F.W.2    Kay, L.E.3
  • 65
    • 0016749447 scopus 로고
    • Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data
    • Strickland S., Palmer G., Massey V. Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data. J. Biol. Chem. 1975, 250:4048-4052.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4048-4052
    • Strickland, S.1    Palmer, G.2    Massey, V.3
  • 67
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    • Tang C., Schwieters C.D., Clore G.M. Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR. Nature 2007, 449:1078-1082.
    • (2007) Nature , vol.449 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, G.M.3
  • 68
    • 70450191983 scopus 로고    scopus 로고
    • Dynamic activation of an allosteric regulatory protein
    • Tzeng S.R., Kalodimos C.G. Dynamic activation of an allosteric regulatory protein. Nature 2009, 462:368-372.
    • (2009) Nature , vol.462 , pp. 368-372
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 69
    • 84894262099 scopus 로고    scopus 로고
    • Essential role of conformational selection in ligand binding
    • Vogt A.D., Pozzi N., Chen Z., Di Cera E. Essential role of conformational selection in ligand binding. Biophys. Chem. 2014, 186:13-21.
    • (2014) Biophys. Chem. , vol.186 , pp. 13-21
    • Vogt, A.D.1    Pozzi, N.2    Chen, Z.3    Di Cera, E.4
  • 70
    • 0038603873 scopus 로고    scopus 로고
    • Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin
    • Weiergräber O.H., Senin I.I., Philippov P.P., Granzin J., Koch K.W. Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin. J. Biol. Chem. 2003, 278:22972-22979.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22972-22979
    • Weiergräber, O.H.1    Senin, I.I.2    Philippov, P.P.3    Granzin, J.4    Koch, K.W.5
  • 71
    • 84922988123 scopus 로고    scopus 로고
    • Conformational selection in protein binding and function
    • Weikl T.R., Paul F. Conformational selection in protein binding and function. Prot. Sci. 2014, 23:1508-1518.
    • (2014) Prot. Sci. , vol.23 , pp. 1508-1518
    • Weikl, T.R.1    Paul, F.2
  • 72
    • 0036774105 scopus 로고    scopus 로고
    • Sense and sensibility in the regulation of voltage-gated Ca(2+) channels
    • Weiss J.L., Burgoyne R.D. Sense and sensibility in the regulation of voltage-gated Ca(2+) channels. Trends Neurosci. 2002, 25:489-491.
    • (2002) Trends Neurosci. , vol.25 , pp. 489-491
    • Weiss, J.L.1    Burgoyne, R.D.2
  • 73
    • 77949587817 scopus 로고    scopus 로고
    • From induced fit to conformational selection: a continuum of binding mechanism controlled by the timescale of conformational transitions
    • Zhou H.X. From induced fit to conformational selection: a continuum of binding mechanism controlled by the timescale of conformational transitions. Biophys. J. 2010, 98:L15-L17.
    • (2010) Biophys. J. , vol.98 , pp. L15-L17
    • Zhou, H.X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.