메뉴 건너뛰기




Volumn 13, Issue 3, 2004, Pages 640-651

Using lanthanide ions to align troponin complexes in solution: Order of lanthanide occupancy in cardiac troponin C

Author keywords

Ion binding order; Lanthanides; NMR; Residual dipolar couplings; Troponin C

Indexed keywords

CALCIUM; CERIUM; LANTHANIDE; PEPTIDE DERIVATIVE; TERBIUM; TROPONIN; TROPONIN C; TROPONIN I; YTTERBIUM;

EID: 1342289296     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03412704     Document Type: Article
Times cited : (10)

References (46)
  • 2
    • 0037093851 scopus 로고    scopus 로고
    • Paramagnetically induced residual dipolar couplings for solution structure determination of lanthanide binding proteins
    • Barbieri, R., Bertini, I., Cavallaro, G., Lee, Y.M., Luchinat, C., and Rosato, A. 2002. Paramagnetically induced residual dipolar couplings for solution structure determination of lanthanide binding proteins. J. Am. Chem. Soc. 124: 5581-5587.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5581-5587
    • Barbieri, R.1    Bertini, I.2    Cavallaro, G.3    Lee, Y.M.4    Luchinat, C.5    Rosato, A.6
  • 6
    • 0033615311 scopus 로고    scopus 로고
    • Measurement of one bond dipolar couplings through lanthanide-induced orientation of a calcium-binding protein
    • Contreras, M.A., Ubach, J., Millet, O., Rizo, J., and Pons, M. 1999. Measurement of one bond dipolar couplings through lanthanide-induced orientation of a calcium-binding protein. J. Am. Chem. Soc. 121: 8947-8948.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8947-8948
    • Contreras, M.A.1    Ubach, J.2    Millet, O.3    Rizo, J.4    Pons, M.5
  • 7
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., 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.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 8
    • 0037064114 scopus 로고    scopus 로고
    • Solution structure of calcium-saturated cardiac troponin C bound to cardiac troponin I
    • Dvoretsky, A., Abusamhadneh, E.M., Howarth, J.W., and Rosevear, P.R. 2002. Solution structure of calcium-saturated cardiac troponin C bound to cardiac troponin I. J. Biol. Chem. 277: 38565-38570.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38565-38570
    • Dvoretsky, A.1    Abusamhadneh, E.M.2    Howarth, J.W.3    Rosevear, P.R.4
  • 9
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah, C.S. and Reinarch, F.C. 1995. The troponin complex and regulation of muscle contraction. FASEB J. 9: 755-767.
    • (1995) FASEB J. , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinarch, F.C.2
  • 10
    • 0034787075 scopus 로고    scopus 로고
    • Calmodulin tagging provides a general method of using lanthanide induced magnetic field orientation to observe residual dipolar couplings in proteins in solution
    • Feeney, J., Birdsall, B., Bradbury, A.F., Biekofsky, R.R., and Bayley, P.M. 2001. Calmodulin tagging provides a general method of using lanthanide induced magnetic field orientation to observe residual dipolar couplings in proteins in solution. J. Biomol. NMR 21: 41-48.
    • (2001) J. Biomol. NMR , vol.21 , pp. 41-48
    • Feeney, J.1    Birdsall, B.2    Bradbury, A.F.3    Biekofsky, R.R.4    Bayley, P.M.5
  • 11
    • 0029088936 scopus 로고
    • Structures of the troponin C regulatory domains in the apo and calcium-saturated states
    • Gagné, S.M., Tsuda, S., Li, M.X., Smillie, L.B., and Sykes, B.D. 1995. Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Nat. Struct. Biol. 2: 784-789.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 784-789
    • Gagné, S.M.1    Tsuda, S.2    Li, M.X.3    Smillie, L.B.4    Sykes, B.D.5
  • 13
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves, M.A. and Holmes, K.C. 1999. Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68: 687-728.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 14
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A.M., Homsher, E., and Regnier, M. 2000. Regulation of contraction in striated muscle. Physiol. Rev. 80: 853-924.
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 15
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson, A.J. and Blevins, R.A. 1994. NMR View: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4: 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, A.J.1    Blevins, R.A.2
  • 17
    • 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
  • 18
    • 0028171882 scopus 로고    scopus 로고
    • Disparate contributions of Tyr10 and Tyr109 to fluorescence intensity of rabbit skeletal muscle troponin C identified using a genetically engineered mutant
    • Keleti, D., Rao, V.G., Su, H., Akella, A.B., Ding, X.L., and Gulati, J. Disparate contributions of Tyr10 and Tyr109 to fluorescence intensity of rabbit skeletal muscle troponin C identified using a genetically engineered mutant. FEBS Lett. 354: 135-139.
    • FEBS Lett. , vol.354 , pp. 135-139
    • Keleti, D.1    Rao, V.G.2    Su, H.3    Akella, A.B.4    Ding, X.L.5    Gulati, J.6
  • 19
    • 0018987046 scopus 로고
    • Terbium binding to troponin-C: Binding stoichiometry and structural-changes induced in the protein
    • Leavis, P.C., Nagy, B., Lehrer, S.S., Bialkowska, H., and Gergely, J. 1980. Terbium binding to troponin-C: Binding stoichiometry and structural-changes induced in the protein. Arch. Biochem. Biophys. 200: 17-21.
    • (1980) Arch. Biochem. Biophys. , vol.200 , pp. 17-21
    • Leavis, P.C.1    Nagy, B.2    Lehrer, S.S.3    Bialkowska, H.4    Gergely, J.5
  • 20
    • 0021102435 scopus 로고
    • Use of lanthanide-induced nuclear magnetic-resonance shifts for determination of protein-structure in solution: EF calcium-binding site of carp parvalbumin
    • Lee, L. and Sykes, B.D. 1983. Use of lanthanide-induced nuclear magnetic-resonance shifts for determination of protein-structure in solution: EF calcium-binding site of carp parvalbumin. Biochemistry 22: 4366-4373.
    • (1983) Biochemistry , vol.22 , pp. 4366-4373
    • Lee, L.1    Sykes, B.D.2
  • 22
    • 0033614841 scopus 로고    scopus 로고
    • 147-163 induces a structural opening in human cardiac troponin-C
    • 147-163 induces a structural opening in human cardiac troponin-C. Biochemistry 38: 8289-8298.
    • (1999) Biochemistry , vol.38 , pp. 8289-8298
    • Li, M.X.1    Spyracopoulos, L.2    Sykes, B.D.3
  • 23
    • 0036655688 scopus 로고    scopus 로고
    • Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin C using NMR spectroscopy
    • Li, M.X., Saude, E.J., Wang, X., Pearlstone, J.R., Smilie, L.B., and Sykes, B.D. 2002. Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin C using NMR spectroscopy. Eur. Biophys. J. 31: 245-256.
    • (2002) Eur. Biophys. J. , vol.31 , pp. 245-256
    • Li, M.X.1    Saude, E.J.2    Wang, X.3    Pearlstone, J.R.4    Smilie, L.B.5    Sykes, B.D.6
  • 24
    • 0038711690 scopus 로고    scopus 로고
    • Structure and dynamics of the C-domain of human cardiac troponin C in complex with the inhibitory region of human cardiac troponin I
    • Lindhout, D.A. and Sykes, B.D. 2003. Structure and dynamics of the C-domain of human cardiac troponin C in complex with the inhibitory region of human cardiac troponin I. J. Biol. Chem. 29: 27024-27034.
    • (2003) J. Biol. Chem. , vol.29 , pp. 27024-27034
    • Lindhout, D.A.1    Sykes, B.D.2
  • 25
    • 0037062556 scopus 로고    scopus 로고
    • Effects of T142 Phosphorylation and mutation R145G on the interaction of the inhibitory region of human cardiac troponin I with the C-domain of human cardiac troponin C
    • Lindhout, D.A., Li, M.X., Schieve, D., and Sykes, B.D. 2002. Effects of T142 Phosphorylation and mutation R145G on the interaction of the inhibitory region of human cardiac troponin I with the C-domain of human cardiac troponin C. Biochemistry 41: 7267-7274.
    • (2002) Biochemistry , vol.41 , pp. 7267-7274
    • Lindhout, D.A.1    Li, M.X.2    Schieve, D.3    Sykes, B.D.4
  • 26
    • 0042844586 scopus 로고    scopus 로고
    • High-yield expression of isotopically labeled peptides for use in NMR studies
    • Lindhout, D.A., Thiessen, A., Schieve, D., and Sykes, B.D. 2003. High-yield expression of isotopically labeled peptides for use in NMR studies. Protein Sci. 12: 1786-1791.
    • (2003) Protein Sci. , vol.12 , pp. 1786-1791
    • Lindhout, D.A.1    Thiessen, A.2    Schieve, D.3    Sykes, B.D.4
  • 28
    • 0034680341 scopus 로고    scopus 로고
    • 2+ and troponin I peptide binding to the E41A mutant of the N-domain of skeletal troponin C
    • 2+ and troponin I peptide binding to the E41A mutant of the N-domain of skeletal troponin C. Biochemistry 39: 12731-12738.
    • (2000) Biochemistry , vol.39 , pp. 12731-12738
    • McKay, R.T.1    Saltibus, L.F.2    Li, M.X.3    Sykes, B.D.4
  • 29
    • 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. Res. 131: 373-378.
    • (1998) J. Magn. Res. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 30
    • 0033919516 scopus 로고    scopus 로고
    • A set of HNCO-based experiments for measurement of residual dipolar couplings in N-15, C-13, (H-2)-labeled proteins
    • Permi, P., Rosevear, P.R., and Annila, A. 2000. A set of HNCO-based experiments for measurement of residual dipolar couplings in N-15, C-13, (H-2)-labeled proteins. J. Biomol. NMR 17: 43-54.
    • (2000) J. Biomol. NMR , vol.17 , pp. 43-54
    • Permi, P.1    Rosevear, P.R.2    Annila, A.3
  • 31
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Potter, J.D. and Gergley, J. 1975. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250: 4628-4633.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4628-4633
    • Potter, J.D.1    Gergley, J.2
  • 32
    • 0024413451 scopus 로고
    • Site-directed mutation of the trigger calcium-binding sites in cardiac troponin C
    • Putkey, J.A., Sweeney, H.L., and Campbell, S.T. 1989. Site-directed mutation of the trigger calcium-binding sites in cardiac troponin C. J. Biol. Chem. 264: 12370-12378.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12370-12378
    • Putkey, J.A.1    Sweeney, H.L.2    Campbell, S.T.3
  • 34
    • 0026444089 scopus 로고
    • Isolation, expression, and mutation of a rabbit skeletal muscle cDNA clone for troponin I
    • Sheng, Z., Pan, B.S., Miller, T., and Potter, J.D. 1992. Isolation, expression, and mutation of a rabbit skeletal muscle cDNA clone for troponin I. J. Biol. Chem. 267: 25407-25413.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25407-25413
    • Sheng, Z.1    Pan, B.S.2    Miller, T.3    Potter, J.D.4
  • 36
    • 0028891899 scopus 로고
    • NMR solution structure of calcium-saturated skeletal muscle troponin C
    • Slupsky, C.M. and Sykes, B.D. 1995. NMR solution structure of calcium-saturated skeletal muscle troponin C. Biochemistry 34: 15953-15964.
    • (1995) Biochemistry , vol.34 , pp. 15953-15964
    • Slupsky, C.M.1    Sykes, B.D.2
  • 37
    • 0010382141 scopus 로고
    • HPLC of peptides and proteins: Separation, analysis, and conformation
    • (eds. C. Mant and R. Hodges). CRC Press, Boca Raton, FL
    • Smillie, L.B. and Nattriss, M. 1990. HPLC of peptides and proteins: Separation, analysis, and conformation. In Amino acid analyses of proteins and peptides: An overview (eds. C. Mant and R. Hodges), pp. 809-821. CRC Press, Boca Raton, FL.
    • (1990) Amino Acid Analyses of Proteins and Peptides: An Overview , pp. 809-821
    • Smillie, L.B.1    Nattriss, M.2
  • 38
    • 0032494188 scopus 로고    scopus 로고
    • Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments
    • Solaro, R.J. and Rarick, H.M. 1998. Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments. Circ. Res. 83: 471-480.
    • (1998) Circ. Res. , vol.83 , pp. 471-480
    • Solaro, R.J.1    Rarick, H.M.2
  • 39
    • 0030856717 scopus 로고    scopus 로고
    • Calcium-induced structural transition in the regulatory domain of human cardiac troponin C
    • Spyracopoulos, L., Li, M.X., Sia, S.K., Gagné, S.M., Chandra, M., Solaro, R.J., and Sykes, B.D. 1997. Calcium-induced structural transition in the regulatory domain of human cardiac troponin C. Biochemistry 36: 12138-12146.
    • (1997) Biochemistry , vol.36 , pp. 12138-12146
    • Spyracopoulos, L.1    Li, M.X.2    Sia, S.K.3    Gagné, S.M.4    Chandra, M.5    Solaro, R.J.6    Sykes, B.D.7
  • 40
    • 0000264741 scopus 로고    scopus 로고
    • Structure of skeletal troponin-C in complex with skeletal troponin-I 115-131: Comparison to cardiac troponin-C-troponin-I 147-163 complex
    • Spyracopoulos, L., McKay, R.T., and Sykes, B.D. 2000. Structure of skeletal troponin-C in complex with skeletal troponin-I 115-131: Comparison to cardiac troponin-C-troponin-I 147-163 complex. Biophys. J. 78: 434A.
    • (2000) Biophys. J. , vol.78
    • Spyracopoulos, L.1    McKay, R.T.2    Sykes, B.D.3
  • 41
    • 0030018695 scopus 로고    scopus 로고
    • 15N-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling
    • 15N-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling. J. Am. Chem. Soc. 118: 6264-6272.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6264-6272
    • Tjandra, N.1    Grzesiek, S.2    Bax, A.3
  • 42
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution
    • Tolman, J.R., Flanagan, J.M., Kennedy, M.A., and Prestegard, J.H. 1995. Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution. Proc. Natl. Acad. Sci. 92: 9279-9283.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 9279-9283
    • Tolman, J.R.1    Flanagan, J.M.2    Kennedy, M.A.3    Prestegard, J.H.4
  • 43
    • 0024300799 scopus 로고
    • Nuclear magnetic-resonance study on rabbit skeletal troponin-C: Calcium-induced conformational change
    • Tsuda, S., Hasegawa, Y., Yoshida, M., Yagi, K., and Hikichi, K. 1988. Nuclear magnetic-resonance study on rabbit skeletal troponin-C: Calcium-induced conformational change. Biochemistry 27: 4120-4126.
    • (1988) Biochemistry , vol.27 , pp. 4120-4126
    • Tsuda, S.1    Hasegawa, Y.2    Yoshida, M.3    Yagi, K.4    Hikichi, K.5
  • 44
    • 0016757164 scopus 로고
    • The amino acid sequence of bovine cardiac troponin-C: Comparison with rabbit skeletal troponin-C
    • van Eerd, J.P. and Takahashi, K. 1975. The amino acid sequence of bovine cardiac troponin-C: Comparison with rabbit skeletal troponin-C. Biochem. Biophys. Res. Commun. 64: 122-127.
    • (1975) Biochem. Biophys. Res. Commun. , vol.64 , pp. 122-127
    • Van Eerd, J.P.1    Takahashi, K.2
  • 46
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR 4: 845-858.
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.