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Volumn 44, Issue 23, 2005, Pages 8267-8273

The effects of Ca2+ binding on the dynamic properties of a designed Ca2+-binding protein

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; SIGNALING;

EID: 20444408057     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050463n     Document Type: Article
Times cited : (15)

References (55)
  • 1
    • 0032531818 scopus 로고    scopus 로고
    • Calcium - A life and death signal
    • Berridge, M. J., Bootman, M. D., and Lipp, P. (1998) Calcium - a life and death signal, Nature 395, 645-648.
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 2
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker, J. P. (1991) Structural aspects of metal liganding to functional groups in proteins. Adv. Protein Chem. 42, 1-76.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 1-76
    • Glusker, J.P.1
  • 5
    • 0033988897 scopus 로고    scopus 로고
    • Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex
    • Lee, A. L., Kinnear, S. A., and Wand, A. J. (2000) Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex, Nat. Struct. Biol. 7, 72-77.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 72-77
    • Lee, A.L.1    Kinnear, S.A.2    Wand, A.J.3
  • 6
    • 0032558982 scopus 로고    scopus 로고
    • Dynamics and thermodynamics of the regulatory domain of human cardiac troponin C in the apo- and calcium-saturated states
    • Spyracopoulos, L., Gagne, S. M., Li, M. X., and Sykes, B. D. (1998) Dynamics and thermodynamics of the regulatory domain of human cardiac troponin C in the apo- and calcium-saturated states, Biochemistry 37, 18032-18044.
    • (1998) Biochemistry , vol.37 , pp. 18032-18044
    • Spyracopoulos, L.1    Gagne, S.M.2    Li, M.X.3    Sykes, B.D.4
  • 9
    • 18844478967 scopus 로고    scopus 로고
    • Backbone and methyl dynamics of the regulatory domain of troponin C: Anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity
    • Gagne, S. M., Tsuda, S., Spyracopoulos, L., Kay, L. E., and Sykes, B. D. (1998) Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity, J. Mol. Biol. 278, 667-686.
    • (1998) J. Mol. Biol. , vol.278 , pp. 667-686
    • Gagne, S.M.1    Tsuda, S.2    Spyracopoulos, L.3    Kay, L.E.4    Sykes, B.D.5
  • 10
    • 0034868445 scopus 로고    scopus 로고
    • NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding
    • Stone, M. J. (2001) NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding, Acc. Chem. Res. 34, 379-388.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 379-388
    • Stone, M.J.1
  • 11
    • 0034719161 scopus 로고    scopus 로고
    • Characterization of the EGF-like module pair 3-4 from vitamin K-dependent protein S using NMR spectroscopy reveals dynamics on three separate time scales and extensive effects from calcium binding
    • Muranyi, A., Evenas, J., Stenberg, Y., Stenflo, J., and Drakenberg, T. (2000) Characterization of the EGF-like module pair 3-4 from vitamin K-dependent protein S using NMR spectroscopy reveals dynamics on three separate time scales and extensive effects from calcium binding, Biochemistry 39, 15742-15756.
    • (2000) Biochemistry , vol.39 , pp. 15742-15756
    • Muranyi, A.1    Evenas, J.2    Stenberg, Y.3    Stenflo, J.4    Drakenberg, T.5
  • 12
    • 3242716711 scopus 로고    scopus 로고
    • N-Terminal domain linkage modulates the folding properties of protein S epidermal growth factor-like modules
    • Kurniawan, N. D., O'Leary, J. M., Thamlitz, A. M., Sofair, R., Werner, J. M., Stenflo, J., and Downing, A. K. (2004) N-Terminal domain linkage modulates the folding properties of protein S epidermal growth factor-like modules. Biochemistry 43, 9352-9360.
    • (2004) Biochemistry , vol.43 , pp. 9352-9360
    • Kurniawan, N.D.1    O'Leary, J.M.2    Thamlitz, A.M.3    Sofair, R.4    Werner, J.M.5    Stenflo, J.6    Downing, A.K.7
  • 13
    • 0035839042 scopus 로고    scopus 로고
    • NMR structure and backbone dynamics of a concatemer of epidermal growth factor homology modules of the human low-density lipoprotein receptor
    • Kurniawan, N. D., Aliabadizadeh, K., Brereton, I. M., Kroon, P. A., and Smith, R. (2001) NMR structure and backbone dynamics of a concatemer of epidermal growth factor homology modules of the human low-density lipoprotein receptor, J. Mol. Biol. 311, 341-356.
    • (2001) J. Mol. Biol. , vol.311 , pp. 341-356
    • Kurniawan, N.D.1    Aliabadizadeh, K.2    Brereton, I.M.3    Kroon, P.A.4    Smith, R.5
  • 14
    • 0012955959 scopus 로고    scopus 로고
    • Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1
    • Smallridge, R. S., Whiteman, P.. Werner, J. M., Campbell, I. D., Handford, P. A., and Downing, A. K. (2003) Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1, J. Biol. Chem. 278, 12199-12206.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12199-12206
    • Smallridge, R.S.1    Whiteman, P.2    Werner, J.M.3    Campbell, I.D.4    Handford, P.A.5    Downing, A.K.6
  • 15
    • 0034598951 scopus 로고    scopus 로고
    • Backbone dynamics of a cbEGF domain pair in the presence of calcium
    • Werner, J. M., Knott, V., Handford, P. A., Campbell, I. D., and Downing, A. K. (2000) Backbone dynamics of a cbEGF domain pair in the presence of calcium, J. Mol. Biol. 296, 1065-1078.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1065-1078
    • Werner, J.M.1    Knott, V.2    Handford, P.A.3    Campbell, I.D.4    Downing, A.K.5
  • 16
    • 0022360904 scopus 로고
    • The cell surface molecule recognized by the erythrocyte receptor of T lymphocytes. Identification and partial characterization using a monoclonal antibody
    • Hunig, T. (1985) The cell surface molecule recognized by the erythrocyte receptor of T lymphocytes. Identification and partial characterization using a monoclonal antibody, J. Exp. Med. 162, 890-901.
    • (1985) J. Exp. Med. , vol.162 , pp. 890-901
    • Hunig, T.1
  • 18
    • 0029930984 scopus 로고    scopus 로고
    • The structure and ligand interactions of CD2: Implications for T-cell function
    • Davis, S. J., and van der Merwe, P. A. (1996) The structure and ligand interactions of CD2: implications for T-cell function, Immunol. Today 17, 177-187.
    • (1996) Immunol. Today , vol.17 , pp. 177-187
    • Davis, S.J.1    Van Der Merwe, P.A.2
  • 19
    • 0030061494 scopus 로고    scopus 로고
    • Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area
    • Dustin, M. L., Ferguson, L. M., Chan, P. Y., Springer, T. A., and Golan, D. E. (1996) Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area, J. Cell Biol. 132, 465-474.
    • (1996) J. Cell Biol. , vol.132 , pp. 465-474
    • Dustin, M.L.1    Ferguson, L.M.2    Chan, P.Y.3    Springer, T.A.4    Golan, D.E.5
  • 21
    • 0029980542 scopus 로고    scopus 로고
    • Structural basis of calcium-induced E-cadherin rigidification and dimerization
    • Nagar, B., Overduin, M., Ikura, M., and Rini, J. M. (1996) Structural basis of calcium-induced E-cadherin rigidification and dimerization, Nature 380, 360-364.
    • (1996) Nature , vol.380 , pp. 360-364
    • Nagar, B.1    Overduin, M.2    Ikura, M.3    Rini, J.M.4
  • 22
    • 0026059140 scopus 로고
    • Structure of domain 1 of rat T lymphocyte CD2 antigen
    • Driscoll, P. C., Cyster, J. G., Campbell, I. D., and Williams, A. F. (1991) Structure of domain 1 of rat T lymphocyte CD2 antigen, Nature 353, 762-765.
    • (1991) Nature , vol.353 , pp. 762-765
    • Driscoll, P.C.1    Cyster, J.G.2    Campbell, I.D.3    Williams, A.F.4
  • 23
    • 0141919670 scopus 로고    scopus 로고
    • Structural biology of the cell adhesion protein CD2: From molecular recognition to protein folding and design
    • Wilkins, A. L., Yang, W., and Yang, J. J. (2003) Structural biology of the cell adhesion protein CD2: from molecular recognition to protein folding and design. Curr. Protein Pept. Sci. 4, 367-373.
    • (2003) Curr. Protein Pept. Sci. , vol.4 , pp. 367-373
    • Wilkins, A.L.1    Yang, W.2    Yang, J.J.3
  • 24
    • 0035042427 scopus 로고    scopus 로고
    • Structural biology of the cell adhesion protein CD2: Alternatively folded states and structure-function relation
    • Yang, J. J., Ye, Y., Carroll, A., Yang, W., and Lee, H. W. (2001) Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation, Curr. Protein Pept. Sci. 2, 1-17.
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 1-17
    • Yang, J.J.1    Ye, Y.2    Carroll, A.3    Yang, W.4    Lee, H.W.5
  • 25
    • 0029140842 scopus 로고
    • Topology of the CD2-CD48 cell-adhesion molecule complex: Implications for antigen recognition by T cells
    • van der Merwe, P. A., McNamee, P. N., Davies, E. A., Barclay, A. N., and Davis, S. J. (1995) Topology of the CD2-CD48 cell-adhesion molecule complex: implications for antigen recognition by T cells, Curr. Biol. 5, 74-84.
    • (1995) Curr. Biol. , vol.5 , pp. 74-84
    • Van Der Merwe, P.A.1    McNamee, P.N.2    Davies, E.A.3    Barclay, A.N.4    Davis, S.J.5
  • 26
    • 0034091784 scopus 로고    scopus 로고
    • A space-time structure determination of human CD2 reveals the CD58-binding mode
    • Kitao, A., and Wagner, G. (2000) A space-time structure determination of human CD2 reveals the CD58-binding mode, Proc. Natl. Acad. Sci. U.S.A. 97, 2064-2068.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2064-2068
    • Kitao, A.1    Wagner, G.2
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0035400194 scopus 로고    scopus 로고
    • Structural basis for the appearance of a molten globule state in chimeric molecules derived from lysozyme and alpha-lactalbumin
    • Joniau, M., Haezebrouck, P., Noyelle, K., and Van Dael, H. (2001) Structural basis for the appearance of a molten globule state in chimeric molecules derived from lysozyme and alpha-lactalbumin, Proteins 44, 1-11.
    • (2001) Proteins , vol.44 , pp. 1-11
    • Joniau, M.1    Haezebrouck, P.2    Noyelle, K.3    Van Dael, H.4
  • 32
    • 0032545295 scopus 로고    scopus 로고
    • 2+ binding site engineered into human lysozyme
    • 2+ binding site engineered into human lysozyme, J. Biol. Chem. 273, 34310-34315.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34310-34315
    • Kuroki, R.1    Yutani, K.2
  • 34
    • 0036656219 scopus 로고    scopus 로고
    • Metal-binding studies for a de novo designed calcium-binding protein
    • Wilkins, A. L., Ye, Y., Yang, W., Lee, H. W., Liu, Z. R., and Yang, J. J. (2002) Metal-binding studies for a de novo designed calcium-binding protein, Protein Eng. 15, 571-574.
    • (2002) Protein Eng. , vol.15 , pp. 571-574
    • Wilkins, A.L.1    Ye, Y.2    Yang, W.3    Lee, H.W.4    Liu, Z.R.5    Yang, J.J.6
  • 35
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity, J. Am. Chem. Soc. 114, 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 36
    • 0001902066 scopus 로고
    • Heteronuclear J-coupling precession during spin-lock and adiabatic pulses-use of adiabatic inversion pulses in high-resolution NMR
    • Bendall, M. R. (1995) Heteronuclear J-coupling precession during spin-lock and adiabatic pulses-use of adiabatic inversion pulses in high-resolution NMR, J. Magn. Reson., Ser. A 116, 46-58.
    • (1995) J. Magn. Reson., Ser. A , vol.116 , pp. 46-58
    • Bendall, M.R.1
  • 37
    • 44049118502 scopus 로고
    • Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanism on the measurement of heteronuclear T1 and T2 values in proteins
    • Kay, L. E., Nicholson, L. K., Delaglio, F., Bax, A., and Torchia, D. A. (1992) Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanism on the measurement of heteronuclear T1 and T2 values in proteins, J. Magn. Reson. 97, 359-375.
    • (1992) J. Magn. Reson. , vol.97 , pp. 359-375
    • Kay, L.E.1    Nicholson, L.K.2    Delaglio, F.3    Bax, A.4    Torchia, D.A.5
  • 40
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G., 3rd. (1995) Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol Biol. 246, 144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer III, A.G.3
  • 41
    • 0034984208 scopus 로고    scopus 로고
    • NMR probes of molecular dynamics: Overview and comparison with other techniques
    • Palmer, A. G., III (2001) NMR probes of molecular dynamics: overview and comparison with other techniques, Annu. Rev. Biophys. Biomol. Struct. 30, 129-155.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 129-155
    • Palmer III, A.G.1
  • 42
    • 3042846786 scopus 로고    scopus 로고
    • Model-free analysis of protein dynamics: Assessment of accuracy and model selection protocols based on molecular dynamics simulation
    • Chen, J., Brooks, C. L., III, and Wright, P. E. (2004) Model-free analysis of protein dynamics: assessment of accuracy and model selection protocols based on molecular dynamics simulation, J. Biomol. NMR 29, 243-257.
    • (2004) J. Biomol. NMR , vol.29 , pp. 243-257
    • Chen, J.1    Brooks III, C.L.2    Wright, P.E.3
  • 43
    • 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., and Kay, L. E. (1996) 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) J. Mol. Biol. , vol.263 , pp. 369-382
    • Yang, D.1    Kay, L.E.2
  • 44
    • 0034723132 scopus 로고    scopus 로고
    • Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters
    • Goodman, J. L., Pagel, M. D., and Stone, M. J. (2000) Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters. J. Mol. Biol. 295, 963-978.
    • (2000) J. Mol. Biol. , vol.295 , pp. 963-978
    • Goodman, J.L.1    Pagel, M.D.2    Stone, M.J.3
  • 45
    • 0030891425 scopus 로고    scopus 로고
    • The counter-receptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions
    • Wyss, D. F., Dayie, K. T., and Wagner, G. (1997) The counter-receptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions, Protein Sci. 6, 534-542.
    • (1997) Protein Sci. , vol.6 , pp. 534-542
    • Wyss, D.F.1    Dayie, K.T.2    Wagner, G.3
  • 47
    • 0032852490 scopus 로고    scopus 로고
    • NMR exchange broadening arising from specific low affinity protein self-association: Analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1
    • Pfuhl, M., Chen, H. A., Kristensen, S. M., and Driscoll, P. C. (1999) NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1, J. Biomol. NMR 14, 307-320.
    • (1999) J. Biomol. NMR , vol.14 , pp. 307-320
    • Pfuhl, M.1    Chen, H.A.2    Kristensen, S.M.3    Driscoll, P.C.4
  • 50
    • 0030473440 scopus 로고    scopus 로고
    • Insights into the local residual entropy of proteins provided by NMR relaxation
    • Li, Z., Raychaudhuri, S., and Wand, A. J. (1996) Insights into the local residual entropy of proteins provided by NMR relaxation, Protein Sci. 5, 2647-2650.
    • (1996) Protein Sci. , vol.5 , pp. 2647-2650
    • Li, Z.1    Raychaudhuri, S.2    Wand, A.J.3
  • 51
    • 34249763437 scopus 로고
    • Backbone dynamics of ribonuclease-T1 and its complex with 2′gmp studied by 2-dimensional heteronuclear NMR-spectroscopy
    • Fushman, D., Weisemann, R., Thuring, H., and Ruterjans, H. (1994) Backbone dynamics of ribonuclease-T1 and its complex with 2′gmp studied by 2-dimensional heteronuclear NMR-spectroscopy, J. Biomol. NMR 4, 61-78.
    • (1994) J. Biomol. NMR , vol.4 , pp. 61-78
    • Fushman, D.1    Weisemann, R.2    Thuring, H.3    Ruterjans, H.4
  • 52
    • 0030299991 scopus 로고    scopus 로고
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: Backbone dynamics and entropy changes of an enzyme upon inhibitor binding
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding, Biochemistry 35, 16036-16047.
    • (1996) Biochemistry , vol.35 , pp. 16036-16047
    • Stivers, J.T.1    Abeygunawardana, C.2    Mildvan, A.S.3
  • 53
    • 0032830040 scopus 로고    scopus 로고
    • Dynamics of stromelysin/inhibitor interactions studied by N-15 NMR relaxation measurements: Comparison of ligand binding to the S-1-S-3 and S-1′-S-3′ subsites
    • Yuan, P., Marshall, V. P., Petzold, G. L., Poorman, R. A., and Stockman, B. J. (1999) Dynamics of stromelysin/inhibitor interactions studied by N-15 NMR relaxation measurements: comparison of ligand binding to the S-1-S-3 and S-1′-S-3′ subsites. J. Biomol. NMR 15, 55-64.
    • (1999) J. Biomol. NMR , vol.15 , pp. 55-64
    • Yuan, P.1    Marshall, V.P.2    Petzold, G.L.3    Poorman, R.A.4    Stockman, B.J.5
  • 54
    • 0032710610 scopus 로고    scopus 로고
    • Increased protein backbone conformational entropy upon hydrophobic ligand binding
    • Zidek, L., Novotny, M. V., and Stone, M. J. (1999) Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nat. Struct. Biol. 6, 1118-11121.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1118-11121
    • Zidek, L.1    Novotny, M.V.2    Stone, M.J.3


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