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Volumn 7, Issue 1, 2000, Pages 72-77

Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; MYOSIN LIGHT CHAIN KINASE;

EID: 0033988897     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/71280     Document Type: Article
Times cited : (323)

References (50)
  • 1
    • 0031567108 scopus 로고    scopus 로고
    • Energetics of target peptide recognition by calmodulin: A calorimetricstudy
    • Wintrode, P.L. & Privalov, P.L. Energetics of target peptide recognition by calmodulin: a calorimetricstudy. J. Mol. Biol. 266.1050-1062 (1997).
    • (1997) J. Mol. Biol. , vol.266 , pp. 1050-1062
    • Wintrode, P.L.1    Privalov, P.L.2
  • 2
    • 0027537127 scopus 로고
    • Structural energetics of peptide recognition: Angiotensin II/antibody binding
    • Murphy, K.P., Xie, D., Garcia, K.C., Amzel, L.M. & Freire, E. Structural energetics of peptide recognition: angiotensin II/antibody binding. Proteins 15, 113-120 (1993).
    • (1993) Proteins , vol.15 , pp. 113-120
    • Murphy, K.P.1    Xie, D.2    Garcia, K.C.3    Amzel, L.M.4    Freire, E.5
  • 3
    • 0027991081 scopus 로고
    • Estimation of changes in side chain configurational entropy in binding and folding: General methods and application to helix formation
    • Lee, K.H., Xie, D., Freire, E. & Amzel, L.M. Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation. Proteins 20, 68-84 (1994).
    • (1994) Proteins , vol.20 , pp. 68-84
    • Lee, K.H.1    Xie, D.2    Freire, E.3    Amzel, L.M.4
  • 5
    • 0000109395 scopus 로고
    • Thermodynamics of the association and the pressure dependence of oligomeric proteins
    • Weber, G. Thermodynamics of the association and the pressure dependence of oligomeric proteins. J. Phys. Chem. 97, 7108-7115 (1993).
    • (1993) J. Phys. Chem. , vol.97 , pp. 7108-7115
    • Weber, G.1
  • 6
    • 0000127140 scopus 로고
    • Method for estimating the configurational entropy of macromolecules
    • Karplus, M. & Kushick, J.N. Method for estimating the configurational entropy of macromolecules. Macromolecules 14, 325-332 (1981).
    • (1981) Macromolecules , vol.14 , pp. 325-332
    • Karplus, M.1    Kushick, J.N.2
  • 7
    • 0028871798 scopus 로고
    • Side-chain conformational entropy in protein folding
    • Doig, A.J. & Sternberg, J.E. Side-chain conformational entropy in protein folding. Protein Sci. 4, 2247-2251 (1995).
    • (1995) Protein Sci. , vol.4 , pp. 2247-2251
    • Doig, A.J.1    Sternberg, J.E.2
  • 8
    • 0026720247 scopus 로고
    • Crystalline ribonuclease a loses function below the dynamical transition at 220 K
    • Rasmussen. B.F., Stock, A.M., Ringe, D. & Petsko, G.A. Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature 357, 423-424 (1992).
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B.F.1    Stock, A.M.2    Ringe, D.3    Petsko, G.A.4
  • 9
    • 0033566242 scopus 로고    scopus 로고
    • Millisecond-timescale motions contribute to the function of the bacterial response regulator protein SpoOF
    • Feher, V.A. & Cavanagh, J. Millisecond-timescale motions contribute to the function of the bacterial response regulator protein SpoOF. Nature 400, 289-293 (1999).
    • (1999) Nature , vol.400 , pp. 289-293
    • Feher, V.A.1    Cavanagh, J.2
  • 10
    • 0033565136 scopus 로고    scopus 로고
    • Relating dynamics to function
    • Stock, A. Relating dynamics to function. Nature400, 221-222 (1999).
    • (1999) Nature , vol.400 , pp. 221-222
    • Stock, A.1
  • 12
    • 0030473440 scopus 로고    scopus 로고
    • Insights into the local entropy of proteins provided by NMR relaxation
    • Li, Z., Raychaudhuri, S. & Wand, A.J. Insights into the local entropy of proteins provided by NMR relaxation. Protein Sci. 5, 2647-2650 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 2647-2650
    • Li, Z.1    Raychaudhuri, S.2    Wand, A.J.3
  • 13
    • 0030601792 scopus 로고    scopus 로고
    • Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding
    • Yang, D. & Kay, LE. Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding. J. Mol. Biol. 263, 369-382 (1996).
    • (1996) J. Mol. Biol. , vol.263 , pp. 369-382
    • Yang, D.1    Kay, L.E.2
  • 14
    • 0028506122 scopus 로고
    • Calmodulin: A versatile calcium mediator protein
    • Vogel, H.J. Calmodulin: a versatile calcium mediator protein. Biochem. Cell Biol. 72, 357-375 (1994).
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 357-375
    • Vogel, H.J.1
  • 15
    • 0021881565 scopus 로고
    • Three-dimensional structure of calmodulin
    • Babu, Y.S. et al. Three-dimensional structure of calmodulin. Nature 315, 37-40 (1985).
    • (1985) Nature , vol.315 , pp. 37-40
    • Babu, Y.S.1
  • 16
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry 31, 5269-5278 (1992).
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 17
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apocalmodulin
    • Zhang, M., Tanaka, T. & Ikura, M. Calcium-induced conformational transition revealed by the solution structure of apocalmodulin. Nature Struct. Biol. 2, 758-767(1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 18
    • 0029159794 scopus 로고
    • Solution structure of calcium-free calmodulin
    • Kuboniwa, H. et al. Solution structure of calcium-free calmodulin. Nature Struct. Biol. 2, 768-776(1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 768-776
    • Kuboniwa, H.1
  • 19
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensionalNMR
    • Ikura, M. et al Solution structure of a calmodulin-target peptide complex by multidimensionalNMR. Science 256, 632-638 (1992).
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1
  • 20
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 a structure of a calmodulin-peptide complex
    • Meador, W.E, Means, A.R. & Quiocho, F.A. Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science 257, 1251-1256 (1992).
    • (1992) Science , vol.257 , pp. 1251-1256
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 21
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures
    • Meador, W.E, Means, A.R. & Quiocho, F.A. Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures. Science 262, 1718-1721 (1993).
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 22
    • 0032834002 scopus 로고    scopus 로고
    • 2+-calmodulin-dependent kinase kinase
    • 2+-calmodulin-dependent kinase kinase. Nature Struct. Biol. 6, 819-824 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 819-824
    • Osawa, M.1
  • 24
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G. & Szabo, A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104, 4546-4559 (1982).
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 25
    • 0033620360 scopus 로고    scopus 로고
    • Comparison of !H and C NMR relaxation techniques for the study of protein methyl group dynamics in solution
    • Lee, A.L, Flynn, P.P. & Wand, A.J. Comparison of !H and C NMR relaxation techniques for the study of protein methyl group dynamics in solution. J. Am. Chem. Soc. 121, 2891-2902 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2891-2902
    • Lee, A.L.1    Flynn, P.P.2    Wand, A.J.3
  • 26
    • 0022549779 scopus 로고
    • Calmodulin binding domains: Characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase
    • Lukas, T.J, Burgess, W.H, Prendergast, F.G, Lau, W. & Watterson, D.M. Calmodulin binding domains: characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase. Biochemistry 25, 1458-1464 (1987).
    • (1987) Biochemistry , vol.25 , pp. 1458-1464
    • Lukas, T.J.1    Burgess, W.H.2    Prendergast, F.G.3    Lau, W.4    Watterson, D.M.5
  • 27
    • 0023664006 scopus 로고
    • The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence. 1
    • Kemp, B.E, Pearson, R.B, Guerriero, V, Bagchi, I.e. & Means, A.R. The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence. 1. Biol. Chem. 262, 2542-2548 (1987).
    • (1987) Biol. Chem. , vol.262 , pp. 2542-2548
    • Kemp, B.E.1    Pearson, R.B.2    Guerriero, V.3    Bagchi, I.E.4    Means, A.R.5
  • 29
    • 0025840594 scopus 로고
    • Structure of the smooth muscle myosin light-chain kinase calmodulin-binding domain peptide bound to calmodulin
    • Roth, S.M. et al. Structure of the smooth muscle myosin light-chain kinase calmodulin-binding domain peptide bound to calmodulin. Biochemistry 30, 10078-10084 (1991).
    • (1991) Biochemistry , vol.30 , pp. 10078-10084
    • Roth, S.M.1
  • 30
    • 0026607148 scopus 로고
    • Characterization of the secondary structure of calmodulin in complex with a calmodulin-binding domain peptide
    • Roth, S.M. et al. Characterization of the secondary structure of calmodulin in complex with a calmodulin-binding domain peptide. Biochemistry 31, 1443-1451 (1992).
    • (1992) Biochemistry , vol.31 , pp. 1443-1451
    • Roth, S.M.1
  • 31
    • 0032991161 scopus 로고    scopus 로고
    • Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure
    • Mittermaier, A., Kay, I.E. & Forman-Kay, J.D. Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure. J. Biol. NMR 13, 181-185 (1999).
    • (1999) J. Biol. NMR , vol.13 , pp. 181-185
    • Mittermaier, A.1    Kay, I.E.2    Forman-Kay, J.D.3
  • 32
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic a-helices
    • O'Neil, K.T. & DeGrado, W.F. How calmodulin binds its targets: sequence independent recognition of amphiphilic a-helices. Trends Biochem. Sci. 15, 59-64 (1990).
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59-64
    • O'Neil, K.T.1    Degrado, W.F.2
  • 33
    • 0025823572 scopus 로고
    • On the role of methionine residues in the sequence -independent recognition of nonpolar protein surfaces
    • Gellman, S.H. On the role of methionine residues in the sequence -independent recognition of nonpolar protein surfaces. Biochemistry 30, 6633-6636 (1991).
    • (1991) Biochemistry , vol.30 , pp. 6633-6636
    • Gellman, S.H.1
  • 34
    • 0029007310 scopus 로고
    • NMR studies of the methionine methyl groups in calmodulin
    • Siivari, K., Zhang, M., Palmer, A.G. & Vogel. HJ. NMR studies of the methionine methyl groups in calmodulin. FEBS Lett. 366, 104-108 (1995).
    • (1995) FEBS Lett. , vol.366 , pp. 104-108
    • Siivari, K.1    Zhang, M.2    Palmer, A.G.3    Vogel, H.J.4
  • 35
    • 0029803672 scopus 로고    scopus 로고
    • Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases
    • Chin, D. & Means, A.R. Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases. J. Biol. Chem. 271, 30465-30471 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 30465-30471
    • Chin, D.1    Means, A.R.2
  • 36
    • 0032055830 scopus 로고    scopus 로고
    • Activation of calcineurin and smooth muscle myosin light chain kinase by Met-to-Leu mutants of calmodulin
    • Edwards, R.A., Walsh, M.P., Sutherland, C. & Vogel, H.J. Activation of calcineurin and smooth muscle myosin light chain kinase by Met-to-Leu mutants of calmodulin. B/ochem. 7. 331, 149-152 (1998).
    • (1998) B/ochem. 7. , vol.331 , pp. 149-152
    • Edwards, R.A.1    Walsh, M.P.2    Sutherland, C.3    Vogel, H.J.4
  • 37
    • 0030042698 scopus 로고    scopus 로고
    • Correlation between dynamics and high affinity binding in an SH2 domain interaction
    • Kay, L.E., Muhandiram, D.R., Farrow, N.A., Aubin, Y. & Forman-Kay, J.D. Correlation between dynamics and high affinity binding in an SH2 domain interaction. Biochemistry 35, 361-368 (1996).
    • (1996) Biochemistry , vol.35 , pp. 361-368
    • Kay, L.E.1    Muhandiram, D.R.2    Farrow, N.A.3    Aubin, Y.4    Forman-Kay, J.D.5
  • 38
    • 0032474462 scopus 로고    scopus 로고
    • Backbone and side chain dynamics of uncomplexed human adipocyte and muscle fatty acid-binding proteins
    • Constantine, K.L. et al. Backbone and side chain dynamics of uncomplexed human adipocyte and muscle fatty acid-binding proteins. Biochemistry 37, 7965-7980 (1998).
    • (1998) Biochemistry , vol.37 , pp. 7965-7980
    • Constantine, K.L.1
  • 39
    • 0029004611 scopus 로고
    • The volume of atoms on the protein surface: Calculated from simulation, using Voronoi polyhedra
    • Gerstein, M., Tsai, J. & Levitt, M. The volume of atoms on the protein surface: calculated from simulation, using Voronoi polyhedra. J. Mol. Eiol. 249, 955-966 (1995).
    • (1995) J. Mol. Eiol. , vol.249 , pp. 955-966
    • Gerstein, M.1    Tsai, J.2    Levitt, M.3
  • 40
    • 0019913548 scopus 로고
    • Inelastic neutron scattering analysis of hexokinase dynamics and its modifacation on binding of glucose
    • Jacrot, B., Cusack, S., Dianoux, A.J. & Engelman, D.M. Inelastic neutron scattering analysis of hexokinase dynamics and its modifacation on binding of glucose. Nature 300, 84-86 (1982).
    • (1982) Nature , vol.300 , pp. 84-86
    • Jacrot, B.1    Cusack, S.2    Dianoux, A.J.3    Engelman, D.M.4
  • 41
    • 0033525126 scopus 로고    scopus 로고
    • Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: Implications for the entropy of association with DNA
    • Bracken, C., Carr, P.A., Cavanagh, J. & Palmer. A.G. Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNA. J. Mol. Biol. 285, 2133-2146 (1999).
    • (1999) J. Mol. Biol. , vol.285 , pp. 2133-2146
    • Bracken, C.1    Carr, P.A.2    Cavanagh, J.3    Palmer, A.G.4
  • 42
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T. & Wells, J.A. A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386 (1995).
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 43
    • 0029058666 scopus 로고
    • Structural analysis of a novel interaction by calmodulin: High-affinity binding of a peptide in the absence of calcium
    • Urbauer, J.L., Short, J.H., Dow, L.K. & Wand, A.J. Structural analysis of a novel interaction by calmodulin: high-affinity binding of a peptide in the absence of calcium. Biochemistry 34, 8099-8109 (1995).
    • (1995) Biochemistry , vol.34 , pp. 8099-8109
    • Urbauer, J.L.1    Short, J.H.2    Dow, L.K.3    Wand, A.J.4
  • 44
    • 0028544153 scopus 로고
    • Resonance assignment of methionine methyl groups and Xs angular information from long-range protoncarbon and carbon-carbon J correlation in a calmodulin-peptide complex
    • Bax, A., Delaglio, F., Grzesiek, 5. & Vuister, G.W. Resonance assignment of methionine methyl groups and Xs angular information from long-range protoncarbon and carbon-carbon J correlation in a calmodulin-peptide complex. J. Biol. NMR 4, 787-797 (1994).
    • (1994) J. Biol. NMR , vol.4 , pp. 787-797
    • Bax, A.1    Delaglio, F.2    Grzesiek, S.3    Vuister, G.W.4
  • 45
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • Bruschweiler, R., Liao, X. & Wright, P.E. Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science 268, 886-889 (1995).
    • (1995) Science , vol.268 , pp. 886-889
    • Bruschweiler, R.1    Liao, X.2    Wright, P.E.3
  • 46
    • 0029550886 scopus 로고
    • Rotational diffusion anisotropy of human ubiquitin from 15N NMR relaxation
    • Tjandra, N., Feller, S.E., Pastor, R.W. S Bax, A. Rotational diffusion anisotropy of human ubiquitin from 15N NMR relaxation. J. Am. Chem.Soc. 117, 12562-12566 (1995).
    • (1995) J. Am. Chem.Soc. , vol.117 , pp. 12562-12566
    • Tjandra, N.1    Feller, S.E.2    Pastor, R.W.S.3    Bax, A.4
  • 47
    • 0031111153 scopus 로고    scopus 로고
    • Rotational anisotropy of proteins from simultaneous analysis of 15N and C, nuclear spin relaxation
    • Lee, L.K., Ranee, M., Chazin, W.J. & Palmer, A.G. Rotational anisotropy of proteins from simultaneous analysis of 15N and C, nuclear spin relaxation. J. Biol. NMR 9, 287-298 (1997).
    • (1997) J. Biol. NMR , vol.9 , pp. 287-298
    • Lee, L.K.1    Ranee, M.2    Chazin, W.J.3    Palmer, A.G.4
  • 48
    • 0033029875 scopus 로고    scopus 로고
    • Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation
    • Lee, A.L. & Wand, A.J. Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation./ Biol. NMR 13, 101-112 (1999).
    • (1999) Biol. NMR , vol.13 , pp. 101-112
    • Lee, A.L.1    Wand, A.J.2
  • 49
    • 0000411902 scopus 로고
    • NMR order parameters of biomolecules: A new analytical representation and application to the Gaussian axial fluctuation model
    • Bruschweiler, R. & Wright, P.E. NMR order parameters of biomolecules: a new analytical representation and application to the Gaussian axial fluctuation model. J. Am. Chem. Soc. 116, 8426-8427 (1994).
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8426-8427
    • Bruschweiler, R.1    Wright, P.E.2
  • 50
    • 0029881007 scopus 로고    scopus 로고
    • A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wuthrich, K. A program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55 (1996).
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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