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Volumn , Issue , 2000, Pages 109-134

Intramolecular dynamics and ligand-induced conformational changes: A stochastic model of receptor action

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EID: 85056068477     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420041873     Document Type: Chapter
Times cited : (3)

References (51)
  • 2
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., Sligar, S. G., and Wolynes, P. G., The energy landscapes and motions of proteins, Science, 254, 1598, 1991.
    • (1991) Science , vol.254 , pp. 1598
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 3
    • 0000364298 scopus 로고
    • The binding potential, a neglected linkage concept
    • Wyman, J., The binding potential, a neglected linkage concept, J. Mol. Biol., 11, 631, 1965.
    • (1965) J. Mol. Biol , vol.11 , pp. 631
    • Wyman, J.1
  • 4
    • 0000977357 scopus 로고
    • Allosteric linkage
    • Wyman, J., Allosteric linkage, J. American Chem. Soc., 89, 2202, 1967.
    • (1967) J. American Chem. Soc , vol.89 , pp. 2202
    • Wyman, J.1
  • 5
    • 70449143838 scopus 로고
    • Interaction at end-plate receptors between different choline derivatives
    • Del Castillo, J. and Katz, B., Interaction at end-plate receptors between different choline derivatives, Proc. R. Soc. Lond. (Biol. Sci.), 146, 369, 1957.
    • (1957) Proc. R. Soc. Lond. (Biol. Sci.) , vol.146 , pp. 369
    • Del Castillo, J.1    Katz, B.2
  • 6
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J. P., On the nature of allosteric transitions: A plausible model, J. Mol. Biol., 12, 88, 1965.
    • (1965) J. Mol. Biol , vol.12 , pp. 88
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 7
    • 0031022024 scopus 로고    scopus 로고
    • Two-state models of protein folding kinetics
    • Zwanzig, R., Two-state models of protein folding kinetics, Proc. Natl. Acad. Sci., 94, 148, 1997.
    • (1997) Proc. Natl. Acad. Sci , vol.94 , pp. 148
    • Zwanzig, R.1
  • 8
    • 0018851861 scopus 로고
    • The role of hormone receptors and GTP-regulatory proteins in membrane transduction
    • Rodbell, M., The role of hormone receptors and GTP-regulatory proteins in membrane transduction, Nature, 284, 17, 1980.
    • (1980) Nature , vol.284 , pp. 17
    • Rodbell, M.1
  • 9
    • 0023062991 scopus 로고
    • G Proteins: Transducers of G protein generated signals
    • Gilman, A. G., G Proteins: transducers of G protein generated signals, Ann. Rev. Biochem., 56, 615, 1987.
    • (1987) Ann. Rev. Biochem , vol.56 , pp. 615
    • Gilman, A.G.1
  • 10
    • 0024284962 scopus 로고
    • Role of G protein subunits in transmembrane signalling
    • Neer, E. J. and Clapham, D. E., Role of G protein subunits in transmembrane signalling, Nature, 333, 129, 1988.
    • (1988) Nature , vol.333 , pp. 129
    • Neer, E.J.1    Clapham, D.E.2
  • 11
    • 0024709982 scopus 로고
    • Signal sorting and amplification through G protein-coupled receptors
    • Ross, E. M., Signal sorting and amplification through G protein-coupled receptors, Neuron, 3, 141, 1989.
    • (1989) Neuron , vol.3 , pp. 141
    • Ross, E.M.1
  • 13
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang, S. R., G protein mechanisms: insights from structural analysis, Ann. Rev. Biochem., 66, 639, 1997.
    • (1997) Ann. Rev. Biochem , vol.66 , pp. 639
    • Sprang, S.R.1
  • 14
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • Bourne, H. R., How receptors talk to trimeric G proteins, Curr. Opin. Cell. Biol., 9, 134, 1997.
    • (1997) Curr. Opin. Cell. Biol , vol.9 , pp. 134
    • Bourne, H.R.1
  • 16
    • 77049220618 scopus 로고
    • Affinity and intrinsic activity in the theory of competitive inhibition
    • Ariëns, E. J., Affinity and intrinsic activity in the theory of competitive inhibition, Arch. Int. Pharmacodyn. Ther., 99, 32, 1954.
    • (1954) Arch. Int. Pharmacodyn. Ther , vol.99 , pp. 32
    • Ariëns, E.J.1
  • 18
    • 85056068016 scopus 로고
    • Theory of drug antagonism
    • Gaddum, J. H., Theory of drug antagonism, Pharmacol. Rev., 9, 21, 1957.
    • (1957) Pharmacol. Rev , vol.9 , pp. 21
    • Gaddum, J.H.1
  • 19
    • 0010673662 scopus 로고
    • A modification of receptor theory
    • Stephenson, R. P., A modification of receptor theory, Br. J. Pharmacol., 11, 379, 1956.
    • (1956) Br. J. Pharmacol , vol.11 , pp. 379
    • Stephenson, R.P.1
  • 20
    • 0000959642 scopus 로고
    • The relationship between chemical structure and biological activity
    • Van Rossum, J. M., The relationship between chemical structure and biological activity, J. Pharm. Pharmacol., 15, 285, 1963.
    • (1963) J. Pharm. Pharmacol , vol.15 , pp. 285
    • Van Rossum, J.M.1
  • 21
    • 0014115893 scopus 로고
    • On the application of “a plausible model” of allosteric proteins to the receptor for acetylcholine
    • Karlin, A., On the application of “a plausible model” of allosteric proteins to the receptor for acetylcholine, J. Theor. Biol., 16, 306, 1967.
    • (1967) J. Theor. Biol , vol.16 , pp. 306
    • Karlin, A.1
  • 22
    • 0015702527 scopus 로고
    • Receptor Mechanisms
    • Rang, H. P., Receptor Mechanisms, Br. J. Pharmacol., 48, 475, 1973.
    • (1973) Br. J. Pharmacol , vol.48 , pp. 475
    • Rang, H.P.1
  • 23
    • 0015535998 scopus 로고
    • On the analysis of pharmacological experiments in terms of an allosteric receptor model
    • Thron, C. D., On the analysis of pharmacological experiments in terms of an allosteric receptor model, Mol. Pharmacol., 9, 1, 1973.
    • (1973) Mol. Pharmacol , vol.9 , pp. 1
    • Thron, C.D.1
  • 24
    • 0002060353 scopus 로고
    • The relationship between classical and cooperative drug action
    • H. P. Rang, Ed., University Park Press, Baltimore
    • Colquhoun, D., The relationship between classical and cooperative drug action, in Drug Receptors, H. P. Rang, Ed., University Park Press, Baltimore, 1973, 149.
    • (1973) Drug Receptors , pp. 149
    • Colquhoun, D.1
  • 25
    • 0021058380 scopus 로고
    • Operational models of pharmacological agonism
    • Black, J. W. and Leff, P., Operational models of pharmacological agonism, Proc. R. Soc. Lond. (Biol. Sci.), 220, 141, 1983.
    • (1983) Proc. R. Soc. Lond. (Biol. Sci.) , vol.220 , pp. 141
    • Black, J.W.1    Leff, P.2
  • 27
    • 0003918423 scopus 로고
    • Chapman and Hall, New York, London
    • Weber, G., Protein Interactions, Chapman and Hall, New York, London, 1992.
    • (1992) Protein Interactions
    • Weber, G.1
  • 28
    • 0026608113 scopus 로고
    • Drug efficacy at guanine nucleotide-binding regulatory protein-linked receptors: Thermodynamic interpretation of negative antagonism and of receptor activity in the absence of ligand
    • Costa, T., Ogino, Y., Munson, P. J., Onaran, H. O., and Rodbard, D., Drug efficacy at guanine nucleotide-binding regulatory protein-linked receptors: thermodynamic interpretation of negative antagonism and of receptor activity in the absence of ligand, Mol. Pharmacol., 41, 549, 1992.
    • (1992) Mol. Pharmacol , vol.41 , pp. 549
    • Costa, T.1    Ogino, Y.2    Munson, P.J.3    Onaran, H.O.4    Rodbard, D.5
  • 29
    • 0027497536 scopus 로고
    • βγ-Subunits of guanine nucleotide-binding proteins and regulation of spontaneous receptor activity: Thermodynamic model for the interaction between receptors and guanine nucleotide-binding protein subunits
    • Onaran, H. O., Costa, T., and Rodbard, D., βγ-Subunits of guanine nucleotide-binding proteins and regulation of spontaneous receptor activity: thermodynamic model for the interaction between receptors and guanine nucleotide-binding protein subunits, Mol. Pharmacol., 43, 245, 1993.
    • (1993) Mol. Pharmacol , vol.43 , pp. 245
    • Onaran, H.O.1    Costa, T.2    Rodbard, D.3
  • 30
    • 0001870572 scopus 로고    scopus 로고
    • Agonist efficacy and allosteric models of receptor action
    • Onaran, H. O. and Costa, T., Agonist efficacy and allosteric models of receptor action, Ann. NY Acad. Sci., 812, 98, 1997.
    • (1997) Ann. NY Acad. Sci , vol.812 , pp. 98
    • Onaran, H.O.1    Costa, T.2
  • 31
    • 0028950255 scopus 로고
    • The two-state model of receptor activation
    • Leff, P., The two-state model of receptor activation, Trends Pharmacol. Sci., 16, 89, 1995.
    • (1995) Trends Pharmacol. Sci , vol.16 , pp. 89
    • Leff, P.1
  • 32
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the β2-adrenergic receptor
    • Samama, P., Cotecchia, S., Costa, T., and Lefkowitz, R. J., A mutation-induced activated state of the β2-adrenergic receptor, J. Biol. Chem., 268, 4625, 1993.
    • (1993) J. Biol. Chem , vol.268 , pp. 4625
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 33
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor
    • De Lean, A., Stadel, J. M., and Lefkowitz, R. J., A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor, J. Biol. Chem., 255, 7108, 1980.
    • (1980) J. Biol. Chem , vol.255 , pp. 7108
    • De Lean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 34
    • 0022408262 scopus 로고
    • The relationship between muscarinic receptor occupancy and adenylate cyclase inhibition in the rabbit myocardium
    • Ehlert, F. J., The relationship between muscarinic receptor occupancy and adenylate cyclase inhibition in the rabbit myocardium, Mol. Pharmacol., 28, 410, 1985.
    • (1985) Mol. Pharmacol , vol.28 , pp. 410
    • Ehlert, F.J.1
  • 35
    • 0015528157 scopus 로고
    • Ligand binding and internal equilibria in proteins
    • Weber, G., Ligand binding and internal equilibria in proteins, Biochemistry, 11, 864, 1972.
    • (1972) Biochemistry , vol.11 , pp. 864
    • Weber, G.1
  • 36
    • 0021697164 scopus 로고
    • The ternary complex model: Its properties and application to ligand interaction with the D2-dopamine receptor of the anterior pituitary gland
    • Wregget, K. A. and DeLean, A., The ternary complex model: Its properties and application to ligand interaction with the D2-dopamine receptor of the anterior pituitary gland, Mol. Pharmacol., 26, 214, 1984.
    • (1984) Mol. Pharmacol , vol.26 , pp. 214
    • Wregget, K.A.1    DeLean, A.2
  • 37
    • 0029935383 scopus 로고    scopus 로고
    • The cubic ternary complex receptor-occupancy model I. model description
    • Weiss, J. M., Morgan, P. H., Lutz, M. W., and Kenakin, T. P., The cubic ternary complex receptor-occupancy model I. model description, J. Theor. Biol., 178, 151, 1996.
    • (1996) J. Theor. Biol , vol.178 , pp. 151
    • Weiss, J.M.1    Morgan, P.H.2    Lutz, M.W.3    Kenakin, T.P.4
  • 38
    • 0021977597 scopus 로고
    • Generalized binding phenomena in an allosteric macromolecule
    • Gill, S. J., Richey, B., Bishop, G., and Wyman, J., Generalized binding phenomena in an allosteric macromolecule, Biophys. Chem., 21, 1, 1985.
    • (1985) Biophys. Chem , vol.21 , pp. 1
    • Gill, S.J.1    Richey, B.2    Bishop, G.3    Wyman, J.4
  • 39
    • 85056043301 scopus 로고    scopus 로고
    • A look into receptor efficacy. From the signalling network of the cell to the intramolecular motion of the receptor
    • Handbook of Experimental Pharmacology, T., Kenakin and J. A., Angus, Eds., Springer Verlag, Heidelberg (in press)
    • Onaran, H. O., Scheer, A., Cotecchia, S., and Costa, T., A look into receptor efficacy. From the signalling network of the cell to the intramolecular motion of the receptor, in General Pharmacology: The Pharmacology of Functional, Biochemical, and Recombinant Receptor Systems, Handbook of Experimental Pharmacology, T., Kenakin and J. A., Angus, Eds., Springer Verlag, Heidelberg (in press).
    • General Pharmacology: The Pharmacology of Functional, Biochemical, and Recombinant Receptor Systems
    • Onaran, H.O.1    Scheer, A.2    Cotecchia, S.3    Costa, T.4
  • 42
    • 0017743694 scopus 로고
    • Relaxation and fluctuation of membrane currents that flow through drug-operated channels
    • Colquhoun, D. and Hawkes, A. G., Relaxation and fluctuation of membrane currents that flow through drug-operated channels, Proc. R. Soc. Lond. B., 199, 231, 1977.
    • (1977) Proc. R. Soc. Lond. B , vol.199 , pp. 231
    • Colquhoun, D.1    Hawkes, A.G.2
  • 43
    • 0001908198 scopus 로고
    • The principles of stochastic interpretation of ionchannel mechanisms
    • B. Sakmann and E. Neher, Eds., Plenum Press, New York
    • Colquhoun, D. and Hawkes, A. G., The principles of stochastic interpretation of ionchannel mechanisms, in Single Channel Recording, B. Sakmann and E. Neher, Eds., Plenum Press, New York, 1983, 135.
    • (1983) Single Channel Recording , pp. 135
    • Colquhoun, D.1    Hawkes, A.G.2
  • 44
    • 0003525155 scopus 로고
    • Proteins: A theoretical perspective of dynamics, structure and thermodynamics
    • I. Prigogine and S. A. Rice, Series Eds., John Wiley & Sons, New York
    • Brooks, C. L., Karplus, M., and Pettit, B. M., Proteins: A theoretical perspective of dynamics, structure and thermodynamics, in Advances in Chemical Physics, Vol. 71, I. Prigogine and S. A. Rice, Series Eds., John Wiley & Sons, New York, 1987.
    • (1987) Advances in Chemical Physics , vol.71
    • Brooks, C.L.1    Karplus, M.2    Pettit, B.M.3
  • 46
    • 0033535839 scopus 로고    scopus 로고
    • Cytochrome b562 folding by electron transfer: Approaching the speed limit for formation of four-helixbundle protein
    • Wittung-Stafshede, P., Lee, J. C., Winkler J. R., and Gray H. B., Cytochrome b562 folding by electron transfer: Approaching the speed limit for formation of four-helixbundle protein, Proc. Natl. Acad. Sci. USA, 96, 6587, 1999.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6587
    • Wittung-Stafshede, P.1    Lee, J.C.2    Winkler, J.R.3    Gray, H.B.4
  • 47
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • Karplus, M. and Petsko, G. A., Molecular dynamics simulations in biology, Nature, 347, 631, 1990.
    • (1990) Nature , vol.347 , pp. 631
    • Karplus, M.1    Petsko, G.A.2
  • 48
    • 36749119688 scopus 로고
    • CO binding to heme proteins: A model for barrier height distributions and slow conformational changes
    • Agmon, N. and Hopfield J. J., CO binding to heme proteins: A model for barrier height distributions and slow conformational changes, J. Chem. Phys., 79, 2042, 1983.
    • (1983) J. Chem. Phys , vol.79 , pp. 2042
    • Agmon, N.1    Hopfield, J.J.2
  • 49
    • 0028856707 scopus 로고
    • Fluorescent labeling of purified β2 adrenergic receptor. Evidence for ligand-specific conformational changes
    • Gether, U., Lin, S., and Kobilka, B. K., Fluorescent labeling of purified β2 adrenergic receptor. Evidence for ligand-specific conformational changes, J. Biol. Chem., 270, 28268, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 28268
    • Gether, U.1    Lin, S.2    Kobilka, B.K.3
  • 50
    • 0029054198 scopus 로고
    • Slow ligand-induced transitions in the allosteric phosphofructokinase from Escherichia coli
    • Auzat, I., Gawlita E., and Garel, J. R., Slow ligand-induced transitions in the allosteric phosphofructokinase from Escherichia coli, J. Mol. Biol., 249, 1995.
    • (1995) J. Mol. Biol , pp. 249
    • Auzat, I.1    Gawlita, E.2    Garel, J.R.3
  • 51
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, A. M., and Chothia, C., Structural mechanisms for domain movements in proteins, Biochemistry, 33, 6739, 1994.
    • (1994) Biochemistry , vol.33 , pp. 6739
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3


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