메뉴 건너뛰기




Volumn 2, Issue 9, 1995, Pages 784-789

Structures of the troponin C regulatory domains in the apo and calcium-saturated states

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; TROPONIN C;

EID: 0029088936     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0995-784     Document Type: Article
Times cited : (251)

References (32)
  • 1
    • 0021151109 scopus 로고
    • Thin filament proteins and thin filament- linked regulation of vertebrate muscle contraction
    • Leavis, P.C. & Gergeley, J. Thin filament proteins and thin filament- linked regulation of vertebrate muscle contraction. CRC Crit. Rev. Biochem. 16, 235-305 (1984).
    • (1984) CRC Crit. Rev. Biochem , vol.16 , pp. 235-305
    • Leavis, P.C.1    Gergeley, J.2
  • 2
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot, A.S. & Potter, J.D. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. A. Rev. Biophys. biophys. Chem. 16, 535-559 (1987).
    • (1987) A. Rev. Biophys. Biophys. Chem , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2
  • 3
    • 0023034376 scopus 로고
    • Regulatory and cytoskeletal proteins of vertebrate skeletal muscle
    • Ohtsuki, I., Maruyama, K. & Ebashi, S. Regulatory and cytoskeletal proteins of vertebrate skeletal muscle. Adv. Protein Chem. 38, 1-67 (1986).
    • (1986) Adv. Protein Chem , vol.38 , pp. 1-67
    • Ohtsuki, I.1    Maruyama, K.2    Ebashi, S.3
  • 4
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah, C.S. & Reinach F.C. The troponin complex and regulation of muscle contraction. FASEB J. in the press (1995).
    • (1995) FASEB J
    • Farah, C.S.1    Reinach, F.C.2
  • 5
    • 0023771079 scopus 로고
    • Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 A resolution
    • Herzberg, O. & James, M.N.G. Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 A resolution. J. molec. Biol. 203, 761-779 (1988).
    • (1988) J. Molec. Biol , vol.203 , pp. 761-779
    • Herzberg, O.1    James, M.N.G.2
  • 6
    • 0023947009 scopus 로고
    • Refined structure of chicken skeletal muscle troponin C in the two- calcium state at 2-Â resolution
    • Satyshur, K.A. et al. Refined structure of chicken skeletal muscle troponin C in the two- calcium state at 2-Â resolution. J. biol. Chem. 263, 1628-1647 (1988).
    • (1988) J. Biol. Chem , vol.263 , pp. 1628-1647
    • Satyshur, K.A.1
  • 8
    • 0028137004 scopus 로고
    • Structural and regulatory functions of the NH2- and COOH-terminal regions of skeletal muscle troponin-l
    • Farah, C.S. ef ai. Structural and regulatory functions of the NH2- and COOH-terminal regions of skeletal muscle troponin-l. J. biol. Chem. 269, 5230-5240 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 5230-5240
    • Farah, C.S.1
  • 9
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin C at 2.8 Â resolution
    • Herzberg, O. & James, M.N.G. Structure of the calcium regulatory muscle protein troponin C at 2.8 Â resolution. Nature 313, 653-659 (1985).
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.G.2
  • 10
    • 0022931544 scopus 로고
    • Model for the Ca2+- induced conformational transition of troponin C
    • Herzberg, O., Moult, J. & James, M.N.G. A model for the Ca2+- induced conformational transition of troponin C. J. biol. Chem. 261, 2638-2644 (1986).
    • (1986) J. Biol. Chem , vol.261 , pp. 2638-2644
    • Herzberg, O.1    Moult, J.2    James, M.3
  • 11
    • 0028670746 scopus 로고
    • Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin C
    • Gagné, S.M. et al. Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin C. Prot. Sci. 3, 1961-1974 (1994).
    • (1994) Prot. Sci , vol.3 , pp. 1961-1974
    • Gagné, S.M.1
  • 12
    • 0028117250 scopus 로고
    • Properties of isolated recombinant N and C domains of chicken troponin C
    • Li, M.X.etal. Properties of isolated recombinant N and C domains of chicken troponin C. Biochemistry 33, 917-925 (1994).
    • (1994) Biochemistry , vol.33 , pp. 917-925
    • Li, M.1
  • 13
    • 0029076557 scopus 로고
    • Calcium- induced dimerization of troponin C: Mode of interaction and use of trifluoroethanol as a dénaturant of quaternary structure
    • Slupsky, C.M., Reinach, F.C., Kay, C.M. & Sykes, B.D. Calcium- induced dimerization of troponin C: mode of interaction and use of trifluoroethanol as a dénaturant of quaternary structure. Biochemistry, 34, 7365-7375 (1995).
    • (1995) Biochemistry , vol.34 , pp. 7365-7375
    • Slupsky, C.M.1    Reinach, F.C.2    Kay, C.M.3    Sykes, B.D.4
  • 14
    • 0027222060 scopus 로고
    • Observation of inter-subunit nuclear Overhauser effects in a dimeric protein
    • Burgering, M.J.M, Boelens, R., Caffrey, M., Breg, J.N. & Kaptein, R. Observation of inter-subunit nuclear Overhauser effects in a dimeric protein. FEBS Lett. 330, 105-109 (1993).
    • (1993) FEBS Lett , vol.330 , pp. 105-109
    • Burgering, M.1    Boelens, R.2    Caffrey, M.3    Breg, J.N.4    Kaptein, R.5
  • 15
    • 84970060791 scopus 로고
    • A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: A program to check the stereochemical quality of protein structures. J. appl. Crystallogr. 26, 283-290 (1993).
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-290
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.4
  • 16
    • 0028181768 scopus 로고    scopus 로고
    • Solution structure of the TR, C fragment of skeletal muscle
    • Findlay, W.A., Sônnichsen, F.D. & Sykes, B.D. Solution structure of the TR, C fragment of skeletal muscle. J. biol. Chem. 269, 6773-6778.
    • J. Biol. Chem , vol.269 , pp. 6773-6778
    • Findlay, W.A.1    Sônnichsen, F.D.2    Sykes, B.D.3
  • 18
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T & Ikura, M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. 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
  • 19
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 A resolution
    • Babu, Y.S., Bugg, C.E. & Cook, W.J. Structure of calmodulin refined at 2.2 A resolution. J. molec. Biol. 203, 191-204 (1988).
    • (1988) J. Molec. Biol , vol.203 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 20
    • 0024447798 scopus 로고
    • Restrained least squares refinement of native (Calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6 A resolution
    • Swain, A.L., Kretsinger, R.H. & Amma, E.L. Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6 A resolution. J. biol. Chem. 264, 16620-16628 (1989).
    • (1989) J. Biol. Chem , vol.264 , pp. 16620-16628
    • Swain, A.L.1    Kretsinger, R.H.E.L.2
  • 21
    • 0025185219 scopus 로고
    • Tructure of oncomodulin refined at 1.85 A resolution. An example of extensive molecular aggregation via Ca2+
    • Ahmed, F.R. eta/. Structure of oncomodulin refined at 1.85 A resolution. An example of extensive molecular aggregation via Ca2+. J. molec. Biol. 216, 127-140 (1990).
    • (1990) J. Molec. Biol , vol.216 , pp. 127-140
    • Ahmed, F.R.1
  • 22
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M. etal. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632-638 (1992).
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1
  • 23
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment, I. ef al. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-58 (1993).
    • (1993) Science , vol.261 , pp. 50-58
    • Rayment, I.1
  • 24
    • 0028211433 scopus 로고
    • Structure of the regulatory domain of scallop myosin at 2.8 A resolution
    • Xie, X. ef al. Structure of the regulatory domain of scallop myosin at 2.8 A resolution. Nature 368, 306-312 (1994).
    • (1994) Nature , vol.368 , pp. 306-312
    • Xie, X.E.A.1
  • 25
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. & Ernst, R.R. Investigation of exchange processes by two dimensional NMR spectroscopy. J. chem. Phys. 71, 4546-4553 (1979).
    • (1979) J. Chem. Phys , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 26
    • 84915716471 scopus 로고
    • Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy
    • Macura, S. & Ernst, R.R. Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy. Molec. Phys. 41, 95-117 (1980).
    • (1980) Molec. Phys , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 27
    • 0003026536 scopus 로고
    • Practical aspects of 3D heteronuclear NMR of proteins
    • Kay, L.E., Marion, D. & Bax, A. Practical aspects of 3D heteronuclear NMR of proteins. J. magn. Res. 84, 72-84 (1989).
    • (1989) J. Magn. Res , vol.84 , pp. 72-84
    • Kay, L.E.1    Marion, D.2    Bax, A.3
  • 28
    • 0001429780 scopus 로고
    • Three-dimensional NOESY-HMQC spectroscopy of a, 3C-labeled protein
    • Ikura, M., Kay, L.E., Tschudin, R. & Bax, A. Three-dimensional NOESY-HMQC spectroscopy of a, 3C-labeled protein. J. magn. Reson. 86, 204-209 (1990).
    • (1990) J. Magn. Reson , vol.86 , pp. 204-209
    • Ikura, M.1    Kay, L.E.2    Tschudin, R.3    Bax, A.4
  • 29
    • 0024396312 scopus 로고
    • Crystal structures of the helixloop-helix calcium- binding proteins. A
    • Strynadka, N.C.J. & James, M.N.G. Crystal structures of the helixloop-helix calcium- binding proteins. A. Rev Biochem. 58, 951-998 (1989).
    • (1989) Rev Biochem , vol.58 , pp. 951-998
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 30
    • 45149137348 scopus 로고
    • New methods for the measurement of NH- CaH coupling constants in l5N-labeled proteins
    • Kay, L.E. & Bax, A. New methods for the measurement of NH- CaH coupling constants in l5N-labeled proteins. J magn. Res. 86, 110- 126 (1990).
    • (1990) J Magn. Res. , vol.86
    • Kay, L.E.1    Bax, A.2
  • 32
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance
    • Havel, T.F. An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance. Prog. Biophys. molec. Biol. 56, 45-78 (1991).
    • (1991) Prog. Biophys. Molec. Biol , vol.56 , pp. 45-78
    • Havel, T.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.