메뉴 건너뛰기




Volumn 9, Issue 2, 2000, Pages 252-264

Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcystin-LR docked complexes

Author keywords

Complex dissociation; Docking; Microcystin LR; NMR; Protein phosphatase 1; Structure based thermodynamics

Indexed keywords

CYANOGINOSIN; PHOSPHOPROTEIN PHOSPHATASE 1;

EID: 0033997037     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.2.252     Document Type: Article
Times cited : (73)

References (56)
  • 1
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptide and proteins
    • Abagyan R, Totrov M. 1994. Biased probability Monte Carlo conformational searches and electrostatic calculations for peptide and proteins. J Mol Biol 235:983-1002.
    • (1994) J Mol Biol , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 2
    • 0011143013 scopus 로고    scopus 로고
    • Loss of translational entropy in binding, folding and catalysis
    • Amzel LM. 1996. Loss of translational entropy in binding, folding and catalysis. Proteins Struct Funct Genet 29:1-6.
    • (1996) Proteins Struct Funct Genet , vol.29 , pp. 1-6
    • Amzel, L.M.1
  • 4
    • 0031040256 scopus 로고    scopus 로고
    • A molecular basis for different interactions of marine toxinse with protein phosphatase-1
    • Bagu JR, Sykes BD, Craig MM, Holmes CFB. 1997. A molecular basis for different interactions of marine toxinse with protein phosphatase-1. J Biol Chem 272:5087-5097.
    • (1997) J Biol Chem , vol.272 , pp. 5087-5097
    • Bagu, J.R.1    Sykes, B.D.2    Craig, M.M.3    Holmes, C.F.B.4
  • 5
    • 0031547981 scopus 로고    scopus 로고
    • Dissecting the energetics of a protein-protein interaction: The binding of ovomucoid third domain to elastase
    • Baker BM, Murphy KP. 1997. Dissecting the energetics of a protein-protein interaction: The binding of ovomucoid third domain to elastase. J Mol Biol 268:557-569.
    • (1997) J Mol Biol , vol.268 , pp. 557-569
    • Baker, B.M.1    Murphy, K.P.2
  • 6
    • 0032311808 scopus 로고    scopus 로고
    • Prediction of binding energetics from structure using empirical parameterization
    • Baker BM, Murphy KP. 1998. Prediction of binding energetics from structure using empirical parameterization. Methods Enzymol 295:295-315.
    • (1998) Methods Enzymol , vol.295 , pp. 295-315
    • Baker, B.M.1    Murphy, K.P.2
  • 7
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin RL. 1986. Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci USA 83:8069-8072.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 8
    • 0030905238 scopus 로고    scopus 로고
    • Structure-based thermodynamic analysis of HIV-1 protease inhibitor
    • Bardi J, Luque I, Freire E. 1997. Structure-based thermodynamic analysis of HIV-1 protease inhibitor. Biochemistry 36:6588-6596.
    • (1997) Biochemistry , vol.36 , pp. 6588-6596
    • Bardi, J.1    Luque, I.2    Freire, E.3
  • 9
  • 10
    • 0030961726 scopus 로고    scopus 로고
    • Entropy in protein folding and in protein-protein interactions
    • Brady GP, Sharp KA. 1997. Entropy in protein folding and in protein-protein interactions. Curr Opin Struct Biol 7:215-221.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 215-221
    • Brady, G.P.1    Sharp, K.A.2
  • 11
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. 1989. The structure and regulation of protein phosphatases. Annu Rev Biochem 58:453-508.
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 12
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • Cooper A. 1976. Thermodynamic fluctuations in protein molecules. Proc Natl Acad Sci USA 73:2740-2741.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 13
    • 0027751617 scopus 로고
    • Identification and characterization of hydrophobic microcystins in canadian freshwater cyanobacteria
    • Craig M, McCready RL, Luu HA, Smillie MA, Dubord P, Holmes CFB. 1993. Identification and characterization of hydrophobic microcystins in canadian freshwater cyanobacteria. Toxicon 31:1541-1549.
    • (1993) Toxicon , vol.31 , pp. 1541-1549
    • Craig, M.1    McCready, R.L.2    Luu, H.A.3    Smillie, M.A.4    Dubord, P.5    Holmes, C.F.B.6
  • 14
    • 0028863592 scopus 로고
    • Atomic solvation parameters in the analysis of protein-protein docking results
    • Cummings MD, Hart TN, Read RJ. 1995. Atomic solvation parameters in the analysis of protein-protein docking results. Protein Sci 4:2087-2099.
    • (1995) Protein Sci , vol.4 , pp. 2087-2099
    • Cummings, M.D.1    Hart, T.N.2    Read, R.J.3
  • 17
    • 0021093448 scopus 로고
    • Enthalpy-entropy compensation and heart capacity changes for protein-ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A
    • Eftink MR, Anusiem AC, Biltonen RL. 1983. Enthalpy-entropy compensation and heart capacity changes for protein-ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A. Biochemistry 22:3884-3896.
    • (1983) Biochemistry , vol.22 , pp. 3884-3896
    • Eftink, M.R.1    Anusiem, A.C.2    Biltonen, R.L.3
  • 18
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • Egloff MP, Cohen PTW, Reinemer P, Barford D. 1995. Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J Mol Biol 254:942-959.
    • (1995) J Mol Biol , vol.254 , pp. 942-959
    • Egloff, M.P.1    Cohen, P.T.W.2    Reinemer, P.3    Barford, D.4
  • 20
    • 0031058541 scopus 로고    scopus 로고
    • The statistical thermodynamic basis for computation of binding affinities: A critical review
    • Gilson MK, Given AG, Bush BL, McCammon JA. 1997. The statistical thermodynamic basis for computation of binding affinities: A critical review. Biophys J 72:1047-1069.
    • (1997) Biophys J , vol.72 , pp. 1047-1069
    • Gilson, M.K.1    Given, A.G.2    Bush, B.L.3    McCammon, J.A.4
  • 21
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/ threonine phosphatase-1
    • Goldberg J, Huang H-B, Kwon Y-B, Greengard P, Nairn AC, Kuriyan J. 1995. Three-dimensional structure of the catalytic subunit of protein serine/ threonine phosphatase-1. Nature 376:745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.-B.2    Kwon, Y.-B.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 22
    • 0029080864 scopus 로고
    • Thermodynamic mapping of the inhibitor site of the aspartic protease endopepstatine
    • Gomez J, Freire E. 1995. Thermodynamic mapping of the inhibitor site of the aspartic protease endopepstatine. J Mol Biol 252:337-350.
    • (1995) J Mol Biol , vol.252 , pp. 337-350
    • Gomez, J.1    Freire, E.2
  • 24
    • 0021749888 scopus 로고
    • Thermodynamic stability and point mutations of bacteriophage T4 lysozyme
    • Hawkes R, Grutter MG, Schellman J. 1984. Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. J Mol Biol 175:195-212.
    • (1984) J Mol Biol , vol.175 , pp. 195-212
    • Hawkes, R.1    Grutter, M.G.2    Schellman, J.3
  • 25
    • 0029957505 scopus 로고    scopus 로고
    • The enthalpy change in protein folding and binding: Refinement of parameters for structure-based calculations
    • Hilser VJ, Gomez J, Freire E. 1996. The enthalpy change in protein folding and binding: Refinement of parameters for structure-based calculations. Proteins Struct Funct Genet 26:123-133.
    • (1996) Proteins Struct Funct Genet , vol.26 , pp. 123-133
    • Hilser, V.J.1    Gomez, J.2    Freire, E.3
  • 26
    • 0029050481 scopus 로고
    • The "cratic correction" and related fallacies
    • Holtzer A. 1995. The "cratic correction" and related fallacies. Biopolymers 35:595-602.
    • (1995) Biopolymers , vol.35 , pp. 595-602
    • Holtzer, A.1
  • 27
    • 0030963598 scopus 로고    scopus 로고
    • Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding
    • Huang H-B, Horiuchi A, Goldberg J, Greengard P, Nairn AC. 1997. Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding. Proc Natl Acad Sci USA 94:3530-3535.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3530-3535
    • Huang, H.-B.1    Horiuchi, A.2    Goldberg, J.3    Greengard, P.4    Nairn, A.C.5
  • 28
    • 0029019869 scopus 로고
    • A continuum model for protein-protein interactions: Application to the docking problem
    • Jackson RM, Sternberg MJE. 1995. A continuum model for protein-protein interactions: Application to the docking problem. J Mol Biol 250:258-275.
    • (1995) J Mol Biol , vol.250 , pp. 258-275
    • Jackson, R.M.1    Sternberg, M.J.E.2
  • 29
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. 1959. Some factors in the interpretation of protein denaturation. Adv Protein Chem 14:1-63.
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 30
    • 0027991081 scopus 로고
    • Estimation of changes in side-chain configurational entropy in binding and folding: General methods and application to helix formation
    • Lee KH, Xie D, Freire E, Amzel LM. 1994. Estimation of changes in side-chain configurational entropy in binding and folding: General methods and application to helix formation. Proteins Struct Funct Genet 20:68-84.
    • (1994) Proteins Struct Funct Genet , vol.20 , pp. 68-84
    • Lee, K.H.1    Xie, D.2    Freire, E.3    Amzel, L.M.4
  • 31
    • 0002889522 scopus 로고
    • The new paradigm for protein research
    • Gregory RB, ed. New York: Marcel Dekker, Inc.
    • Lumry R. 1995. The new paradigm for protein research. In: Gregory RB, ed. Protein-solvent interactions. New York: Marcel Dekker, Inc. pp 1-136.
    • (1995) Protein-solvent Interactions , pp. 1-136
    • Lumry, R.1
  • 32
    • 0014722597 scopus 로고
    • Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous property of water
    • Lumry R, Rajender S. 1970. Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous property of water. Biopolymers 9:1125-1227.
    • (1970) Biopolymers , vol.9 , pp. 1125-1227
    • Lumry, R.1    Rajender, S.2
  • 33
    • 0032318864 scopus 로고    scopus 로고
    • Structure-based prediction of binding affinities and molecular design of peptide ligands
    • Luque I, Freire E. 1998. Structure-based prediction of binding affinities and molecular design of peptide ligands. Methods Enzymol 295:295-315.
    • (1998) Methods Enzymol , vol.295 , pp. 295-315
    • Luque, I.1    Freire, E.2
  • 37
    • 0030914617 scopus 로고    scopus 로고
    • Comparison of database potentials molecular mechanics force fields
    • Moult J. 1997. Comparison of database potentials molecular mechanics force fields. Curr Opin Struct Biol 7:194-199.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 194-199
    • Moult, J.1
  • 38
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behaviour in proteins
    • Murphy KP, Freire E. 1992. Thermodynamics of structural stability and cooperative folding behaviour in proteins. Adv Protein Chem 43:313-361.
    • (1992) Adv Protein Chem , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 40
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct Funct Genet 11:281-296.
    • (1991) Proteins Struct Funct Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 42
    • 0031547977 scopus 로고    scopus 로고
    • Empirical free energy calculations: A blind test and further improvement of the method
    • Novotny J, Bruccoleri RE, Davis M, Sharp KA. 1997. Empirical free energy calculations: A blind test and further improvement of the method. J Mol Biol 268:401-411.
    • (1997) J Mol Biol , vol.268 , pp. 401-411
    • Novotny, J.1    Bruccoleri, R.E.2    Davis, M.3    Sharp, K.A.4
  • 43
    • 0027057360 scopus 로고
    • Hyperphosphorylation of cytokeratins 8 and 18 by microcystin-LR, a new liver tumor promoter, in primary cultured rat hepatocytes
    • Ohta T, Nishiwaki R, Yatsunami J, Komori A, Suganuma M, Fujiki H. 1992. Hyperphosphorylation of cytokeratins 8 and 18 by microcystin-LR, a new liver tumor promoter, in primary cultured rat hepatocytes. Carcinogenesis 13:2443-2447.
    • (1992) Carcinogenesis , vol.13 , pp. 2443-2447
    • Ohta, T.1    Nishiwaki, R.2    Yatsunami, J.3    Komori, A.4    Suganuma, M.5    Fujiki, H.6
  • 44
    • 0027166270 scopus 로고
    • Empirical scale of side-chain conformational entropy in protein folding
    • Pickett S, Sternberg MJE. 1993. Empirical scale of side-chain conformational entropy in protein folding. J Mol Biol 231:825-839.
    • (1993) J Mol Biol , vol.231 , pp. 825-839
    • Pickett, S.1    Sternberg, M.J.E.2
  • 45
    • 0021755764 scopus 로고
    • Solvent accessible surface area and excluded volumes in proteins
    • Richmond TJ. 1984. Solvent accessible surface area and excluded volumes in proteins. J Mol Biol 82:63-89.
    • (1984) J Mol Biol , vol.82 , pp. 63-89
    • Richmond, T.J.1
  • 47
    • 0028170809 scopus 로고
    • Protein serine/threonine phosphatases-new avenues for cell regulation
    • Shenolikar S. 1994. Protein serine/threonine phosphatases-new avenues for cell regulation. Anna Rev Cell Biol 10:55-86.
    • (1994) Anna Rev Cell Biol , vol.10 , pp. 55-86
    • Shenolikar, S.1
  • 48
    • 0024298839 scopus 로고
    • Stability mutants of staphylococcal nuclease: Large compensation enthalpy-entropy changes for the reversible denaturation reaction
    • Shortle D, Meeker AK, Freire E. 1988. Stability mutants of staphylococcal nuclease: Large compensation enthalpy-entropy changes for the reversible denaturation reaction. Biochemistry 27:4761-4768.
    • (1988) Biochemistry , vol.27 , pp. 4761-4768
    • Shortle, D.1    Meeker, A.K.2    Freire, E.3
  • 50
    • 0028950664 scopus 로고
    • Inhibition of specific binding of okadaic acid to protein phosphatase-2A by microcystin-LR, calyculin-A and tautomycin: Method of analysis of interactions of tight-binding ligands with target protein
    • Takai A, Sasaki K, Nagai H, Mieskes G, Isobe M, Isono K, Yasumoto T. 1995. Inhibition of specific binding of okadaic acid to protein phosphatase-2A by microcystin-LR, calyculin-A and tautomycin: Method of analysis of interactions of tight-binding ligands with target protein. Biochem J 306:657-665.
    • (1995) Biochem J , vol.306 , pp. 657-665
    • Takai, A.1    Sasaki, K.2    Nagai, H.3    Mieskes, G.4    Isobe, M.5    Isono, K.6    Yasumoto, T.7
  • 51
    • 0031567782 scopus 로고    scopus 로고
    • The entropy of protein association
    • Tamura A, Privalov PL. 1997. The entropy of protein association. J Mol Biol 273:1048-1060.
    • (1997) J Mol Biol , vol.273 , pp. 1048-1060
    • Tamura, A.1    Privalov, P.L.2
  • 52
    • 0030968991 scopus 로고    scopus 로고
    • Empirical potentials and functions for protein folding and binding
    • Vajda S, Sippl M, Novotny J. 1997. Empirical potentials and functions for protein folding and binding. Curr Opin Struct Biol 7:222-228.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 222-228
    • Vajda, S.1    Sippl, M.2    Novotny, J.3
  • 53
    • 0029933286 scopus 로고    scopus 로고
    • Prediction of complexes using empirical free energy functions
    • Weng Z, Vajda D, DeLesi C. 1996. Prediction of complexes using empirical free energy functions. Protein Sci 5:614-626.
    • (1996) Protein Sci , vol.5 , pp. 614-626
    • Weng, Z.1    Vajda, D.2    Delesi, C.3
  • 55
    • 0027980359 scopus 로고
    • Molecular basis of cooperativity in protein folding. V. Thermodynamic and structural conditions for the stabilization of compact denatured states
    • Xie D, Freire E. 1994. Molecular basis of cooperativity in protein folding. V. Thermodynamic and structural conditions for the stabilization of compact denatured states. Proteins Struct Funct Genet 19:291-301.
    • (1994) Proteins Struct Funct Genet , vol.19 , pp. 291-301
    • Xie, D.1    Freire, E.2
  • 56
    • 0000035228 scopus 로고    scopus 로고
    • Contribution of translational and rotational entropy to the unfolding of a dimeric coiled-coil
    • Yu Y, Lavigne P, Kay CM, Hodges RS, Privalov PL. 1998. Contribution of translational and rotational entropy to the unfolding of a dimeric coiled-coil. J Phys Chem B 103:2270-2278.
    • (1998) J Phys Chem B , vol.103 , pp. 2270-2278
    • Yu, Y.1    Lavigne, P.2    Kay, C.M.3    Hodges, R.S.4    Privalov, P.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.