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Volumn 13, Issue 11, 2004, Pages 2925-2938

NMR and molecular dynamics studies of the interaction of melatonin with calmodulin

Author keywords

Calmodulin; Fluorescence; Melatonin; Molecular dynamics; NMR; Weak interactions

Indexed keywords

CALCIUM; CALMODULIN; MELATONIN;

EID: 7244242651     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04611404     Document Type: Article
Times cited : (45)

References (69)
  • 1
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu, Y.S., Bugg, C.E., and Cook, W.J. 1988. Structure of calmodulin refined at 2.2 Å resolution. J. Mol. Biol. 204: 191-204.
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 2
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • Barbato, G., Ikura, M., Kay, L.E., Pastor, R.W., and Bax, A. 1992. Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible. Biochemistry 31: 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 3
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T., Billeter, M., Güntert, P., and Wüthrich, K. 1995. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 5: 1-10.
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 7
    • 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
  • 10
    • 0036479749 scopus 로고    scopus 로고
    • Melatonin as a chronobiotic/anticancer agent: Cellular, biochemical, and molecular mechanisms of action and their implications for circadian-based cancer therapy
    • Blask, D.E., Sauer, L.A., and Dauchy, R.T. 2002. Melatonin as a chronobiotic/anticancer agent: Cellular, biochemical, and molecular mechanisms of action and their implications for circadian-based cancer therapy. Curr. Top. Med. Chem. 2: 113-132.
    • (2002) Curr. Top. Med. Chem. , vol.2 , pp. 113-132
    • Blask, D.E.1    Sauer, L.A.2    Dauchy, R.T.3
  • 11
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G. and Ruben, D.J. 1980. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69: 185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 12
    • 84986513567 scopus 로고
    • Determining atom-centered monopoles from molecular electrostatic potential: The need for high sampling density in formamide conformational analysis
    • Breneman, C.M. and Wiberg, K.B. 1990. Determining atom-centered monopoles from molecular electrostatic potential: The need for high sampling density in formamide conformational analysis. J. Comput. Chem. 11: 361-373.
    • (1990) J. Comput. Chem. , vol.11 , pp. 361-373
    • Breneman, C.M.1    Wiberg, K.B.2
  • 15
    • 0028558882 scopus 로고
    • Drug binding by calmodulin: Crystal structure of a calmodulin- trifluoperazine complex
    • Cook, W.J., Walter, L.J., and Walter, M.R. 1994. Drug binding by calmodulin: Crystal structure of a calmodulin-trifluoperazine complex. Biochemistry 33: 15259-15265.
    • (1994) Biochemistry , vol.33 , pp. 15259-15265
    • Cook, W.J.1    Walter, L.J.2    Walter, M.R.3
  • 18
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici, A. and Ikura, M. 1995. Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24: 85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 19
    • 0036219437 scopus 로고    scopus 로고
    • Modulation of intracellular calcium and calmodulin by melatonin in MCF-7 human breast cancer cells
    • Dai, J., Inscho, E.W., Yuan, L., and Hill, S.M. 2002. Modulation of intracellular calcium and calmodulin by melatonin in MCF-7 human breast cancer cells. J. Pineal Res. 32: 112-119.
    • (2002) J. Pineal Res. , vol.32 , pp. 112-119
    • Dai, J.1    Inscho, E.W.2    Yuan, L.3    Hill, S.M.4
  • 20
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on unix pipes
    • Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on unix pipes. J. Biomol. NMR 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 22
    • 0025007511 scopus 로고
    • Pharmacology of drugs that alter multidrug resistance in cancer
    • Ford, J.M. and Hait, W.N. 1990. Pharmacology of drugs that alter multidrug resistance in cancer. Pharmacol. Rev. 42: 155-199.
    • (1990) Pharmacol. Rev. , vol.42 , pp. 155-199
    • Ford, J.M.1    Hait, W.N.2
  • 24
    • 0031058541 scopus 로고    scopus 로고
    • The statistical-thermodynamic basis for computation of binding affinities: A critical review
    • Gilson, M.K., Given, J.S., Bush, B.L., and McCammon, J.A. 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, J.S.2    Bush, B.L.3    McCammon, J.A.4
  • 25
    • 0025135112 scopus 로고
    • Automated docking of substrates to proteins by simulated annealing
    • Goodsell, D.S. and Olson, A.J. 1990. Automated docking of substrates to proteins by simulated annealing. Proteins 8: 195-202.
    • (1990) Proteins , vol.8 , pp. 195-202
    • Goodsell, D.S.1    Olson, A.J.2
  • 28
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich, K.P. and Ikura, M. 2002. Calmodulin in action: Diversity in target recognition and activation mechanisms. Cell 108: 739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 30
    • 0028512725 scopus 로고
    • Effects of melatonin on microtubule assembly depend on hormone concentration: Role of melatonin as a calmodulin antagonist
    • Huerto-Delgadillo, L., Anton-Tay, F., and Benitez-King, G. 1994. Effects of melatonin on microtubule assembly depend on hormone concentration: Role of melatonin as a calmodulin antagonist. J. Pineal Res. 17: 55-62.
    • (1994) J. Pineal Res. , vol.17 , pp. 55-62
    • Huerto-Delgadillo, L.1    Anton-Tay, F.2    Benitez-King, G.3
  • 31
    • 0025341339 scopus 로고
    • 15N spectra of larger proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy: Application to calmodulin
    • 15N spectra of larger proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy: Application to calmodulin. Biochemistry 29: 4659-4667.
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 33
    • 36549092795 scopus 로고
    • Efficient computation of absolute free energies of binding by computer simulations. Application to the methane dimer in water
    • Jorgensen, W.L., Buckner, J.K., Boudon, S., and Tirado-Rives, J. 1988. Efficient computation of absolute free energies of binding by computer simulations. Application to the methane dimer in water. J. Chem. Phys. 89: 3742-3746.
    • (1988) J. Chem. Phys. , vol.89 , pp. 3742-3746
    • Jorgensen, W.L.1    Buckner, J.K.2    Boudon, S.3    Tirado-Rives, J.4
  • 36
    • 7044239742 scopus 로고
    • Free energy calculations: Applications to chemical and biochemical problems
    • Kollman, P.A. 1993. Free energy calculations: Applications to chemical and biochemical problems. Chem. Rev. 93: 2395-2417.
    • (1993) Chem. Rev. , vol.93 , pp. 2395-2417
    • Kollman, P.A.1
  • 38
    • 0036262808 scopus 로고    scopus 로고
    • The effect of calmodulin antagonist berbaminederivative-EBB on hepatoma in vitro and in vivo
    • Liu, J., Qi, S., Zhu, H., Zhang, J., Li, Z., and Wang, T. 2002. The effect of calmodulin antagonist berbaminederivative-EBB on hepatoma in vitro and in vivo. Chin. Med. J. (Engl.) 115: 759-762.
    • (2002) Chin. Med. J. (Engl.) , vol.115 , pp. 759-762
    • Liu, J.1    Qi, S.2    Zhu, H.3    Zhang, J.4    Li, Z.5    Wang, T.6
  • 39
    • 0036677555 scopus 로고    scopus 로고
    • On the calculation of absolute macromolecular binding free energies
    • Luo, H. and Sharp, K. 2002. On the calculation of absolute macromolecular binding free energies. Proc. Natl. Acad Sci. 99: 10399-10404.
    • (2002) Proc. Natl. Acad Sci. , vol.99 , pp. 10399-10404
    • Luo, H.1    Sharp, K.2
  • 40
    • 0023940916 scopus 로고
    • Calmodulin antagonists of improved potency and specificity for use in the study of calmodulin biochemistry
    • MacNeil, S., Griffin, M., Cooke, A.M., Pettett, N.J., Dawson, R.A., Owen, R., and Blackburn. G.M. 1988. Calmodulin antagonists of improved potency and specificity for use in the study of calmodulin biochemistry. Biochem. Pharmacol. 37: 1717-1723.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 1717-1723
    • MacNeil, S.1    Griffin, M.2    Cooke, A.M.3    Pettett, N.J.4    Dawson, R.A.5    Owen, R.6    Blackburn, G.M.7
  • 41
    • 0024362326 scopus 로고
    • Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: Application to interleukin
    • Marion, D., Driscoll, P.C., Kay, L.E., Wingfield, P.T., Bax, A., Gronenborn, A.M., and Clore, G.M. 1989. Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: Application to interleukin. Biochemistry 28: 6150-6156.
    • (1989) Biochemistry , vol.28 , pp. 6150-6156
    • Marion, D.1    Driscoll, P.C.2    Kay, L.E.3    Wingfield, P.T.4    Bax, A.5    Gronenborn, A.M.6    Clore, G.M.7
  • 42
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin. 2.4 Å structure of a calmodulin-peptide complex
    • Meador. W.E., Means, A.R., and Quiocho, F.A. 1992. Target enzyme recognition by calmodulin. 2.4 Å structure of a calmodulin-peptide complex. Science 257: 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 43
    • 0027763443 scopus 로고
    • Nuclear localization of melatonin in different mammalian tissues. Immunochemical and radioimmunoassay evidence
    • Menéndez-Pelaez, A., Poeggeler, B., Reiter, R.J., Barion-Waiden, L.R., Pablos, M.I., and Tan, X. 1993. Nuclear localization of melatonin in different mammalian tissues. Immunochemical and radioimmunoassay evidence. J. Cell Biochem. 53: 373-382.
    • (1993) J. Cell Biochem. , vol.53 , pp. 373-382
    • Menéndez-Pelaez, A.1    Poeggeler, B.2    Reiter, R.J.3    Barion-Waiden, L.R.4    Pablos, M.I.5    Tan, X.6
  • 44
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • Mori, S., Abeygunawardana, C., Johnson, M.O., and van Zijl, P.C. 1995. Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J. Magn. Reson. B 108: 94-98.
    • (1995) J. Magn. Reson. B , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Johnson, M.O.3    Van Zijl, P.C.4
  • 45
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Belew, R.K., and Olson, A.J. 1998. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comp. Chem. 19: 1639-1662.
    • (1998) J. Comp. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 46
    • 0024370325 scopus 로고
    • Structural organization of multiple rat calmodulin genes
    • Nojima, H. 1989. Structural organization of multiple rat calmodulin genes. J. Mol. Biol. 208: 269-282.
    • (1989) J. Mol. Biol. , vol.208 , pp. 269-282
    • Nojima, H.1
  • 47
    • 0032512626 scopus 로고    scopus 로고
    • Solution structure of calmodulin-W-7 complex: The basis of diversity in molecular recognition
    • Osawa, M., Swindells, M.B., Tanikawa, J., Tanaka, T., Mase, T., Furuya, T., and Ikura, M. 1998. Solution structure of calmodulin-W-7 complex: The basis of diversity in molecular recognition. J. Mol. Biol. 276: 165-176.
    • (1998) J. Mol. Biol. , vol.276 , pp. 165-176
    • Osawa, M.1    Swindells, M.B.2    Tanikawa, J.3    Tanaka, T.4    Mase, T.5    Furuya, T.6    Ikura, M.7
  • 49
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger, M., Delaglio, F., and Bax, A. 1998. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J. Magn. Reson. 131: 373-378.
    • (1998) J. Magn. Reson. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 50
    • 0032478157 scopus 로고    scopus 로고
    • Melatotin and serotonin interactions with calmodulin: NMR, spectroscopic and biochemical studies
    • Ouyang, H. and Vogel, H.J. 1998. Melatotin and serotonin interactions with calmodulin: NMR, spectroscopic and biochemical studies. Biochim. Biophys. Acta 1383: 37-47.
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 37-47
    • Ouyang, H.1    Vogel, H.J.2
  • 51
    • 0026951903 scopus 로고
    • Gradient tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenár, V. 1992. Gradient tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenár, V.3
  • 52
    • 0030930937 scopus 로고    scopus 로고
    • Inhibition of cerebellar nitric oxide synthase and cyclic GMP production by melatonin via complex formation with calmodulin
    • Pozo, D., Reiter, R.J., Calvo, J.R., and Guerrero, J.M. 1997. Inhibition of cerebellar nitric oxide synthase and cyclic GMP production by melatonin via complex formation with calmodulin. J. Cell. Biochem. 65: 430-442.
    • (1997) J. Cell. Biochem. , vol.65 , pp. 430-442
    • Pozo, D.1    Reiter, R.J.2    Calvo, J.R.3    Guerrero, J.M.4
  • 53
    • 0019980821 scopus 로고
    • Inhibition of calmodulin by phenothiazines and related drugs: Structure-activity relationships
    • Prozialeck, W.C. and Weiss, B. 1982. Inhibition of calmodulin by phenothiazines and related drugs: Structure-activity relationships. J. Pharmacol. Exp. Ther. 222: 509-516.
    • (1982) J. Pharmacol. Exp. Ther. , vol.222 , pp. 509-516
    • Prozialeck, W.C.1    Weiss, B.2
  • 54
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.P., Ciccotti, G., and Berendsen, H.J.C. 1977. Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes. J. Comp. Phys. 23: 327-341.
    • (1977) J. Comp. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 56
    • 13444269041 scopus 로고
    • Computer optimized decoupling scheme for wideband applications and low-level operation
    • Shaka, A.J., Barker, P.B., and Freeman, R. 1985. Computer optimized decoupling scheme for wideband applications and low-level operation. J. Magn. Reson. 64: 547-552.
    • (1985) J. Magn. Reson. , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 57
    • 0001350902 scopus 로고
    • Gradient-tailored water suppression for 1H-15N HSQC experiments optimized to retain full sensitivity
    • Sklenár, V., Piotto, M., Leppik, R., and Saudek, V. 1993. Gradient-tailored water suppression for 1H-15N HSQC experiments optimized to retain full sensitivity. J. Magn. Reson. Series A 102: 241-245.
    • (1993) J. Magn. Reson. Series A , vol.102 , pp. 241-245
    • Sklenár, V.1    Piotto, M.2    Leppik, R.3    Saudek, V.4
  • 58
    • 0025719432 scopus 로고
    • Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-Å resolution
    • Taylor, D.A., Sack, J.S., Maune, J.F., Beckingham, K., and Quiocho, F.A. 1991. Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-Å resolution. J. Biol. Chem. 266: 21375-21380.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21375-21380
    • Taylor, D.A.1    Sack, J.S.2    Maune, J.F.3    Beckingham, K.4    Quiocho, F.A.5
  • 61
    • 0019947482 scopus 로고
    • Interaction of drugs with calmodulin. Biochemical, pharmacological and clinical implications
    • Weiss, B., Prozialeck, W.C., and Wallace, T.L. 1982. Interaction of drugs with calmodulin. Biochemical, pharmacological and clinical implications. Biochem. Pharmacol. 31: 2217-2226.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 2217-2226
    • Weiss, B.1    Prozialeck, W.C.2    Wallace, T.L.3
  • 64
    • 0032584749 scopus 로고    scopus 로고
    • Lack of calmodulin antagonism of melatonin in T-lymphocyte activation
    • Wolfler, A., Schauenstein, K., and Liebmann, P.M. 1998. Lack of calmodulin antagonism of melatonin in T-lymphocyte activation. Life Sci. 63: 835-842.
    • (1998) Life Sci. , vol.63 , pp. 835-842
    • Wolfler, A.1    Schauenstein, K.2    Liebmann, P.M.3
  • 66
    • 0035115805 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the calmodulin-trifluoperazine complex in aqueos solution
    • Yamaotsu, N., Suga, M., and Hirono, S. 2001. Molecular dynamics simulation of the calmodulin-trifluoperazine complex in aqueos solution. Biopolymers 58: 410-421.
    • (2001) Biopolymers , vol.58 , pp. 410-421
    • Yamaotsu, N.1    Suga, M.2    Hirono, S.3
  • 67
    • 0025204231 scopus 로고
    • Differential inhibition of calcium-dependent and calmodulin-dependent enzymes by drug-calmodulin adducts
    • Zhang, S.P., Prozialeck, W.C., and Weiss, B. 1990. Differential inhibition of calcium-dependent and calmodulin-dependent enzymes by drug-calmodulin adducts. Mol. Pharmacol. 38: 698-704.
    • (1990) Mol. Pharmacol. , vol.38 , pp. 698-704
    • Zhang, S.P.1    Prozialeck, W.C.2    Weiss, B.3
  • 68
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E.R.P. 2002. Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 41: 1-7.
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.P.1
  • 69
    • 0024595889 scopus 로고
    • Heteronuclear three dimensional NMR spectroscopy of the inflammatory protein C5a
    • Zuiderweg, E.R.P. and Fesik, S.W. 1989. Heteronuclear three dimensional NMR spectroscopy of the inflammatory protein C5a. Biochemistry 28: 2387-2391.
    • (1989) Biochemistry , vol.28 , pp. 2387-2391
    • Zuiderweg, E.R.P.1    Fesik, S.W.2


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