메뉴 건너뛰기




Volumn 54, Issue SUPPL. 1, 2005, Pages

Crystal structure of troponin and the molecular mechanism of muscle regulation

Author keywords

Calcium; EF hand; Muscle regulation; Synchrotron; Troponin; X ray crystallography

Indexed keywords

CALCIUM; TROPONIN; TROPONIN C; TROPONIN I; TROPONIN T;

EID: 33750223984     PISSN: 00220744     EISSN: 14779986     Source Type: Journal    
DOI: 10.1093/jmicro/54.suppl_1.i35     Document Type: Conference Paper
Times cited : (10)

References (27)
  • 1
    • 0014396206 scopus 로고
    • Calcium ion and muscle contraction
    • Ebashi S and Endo M (1968) Calcium ion and muscle contraction. Prog. Biophys. Mol. Biol. 18: 123-183.
    • (1968) Prog. Biophys. Mol. Biol. , vol.18 , pp. 123-183
    • Ebashi, S.1    Endo, M.2
  • 2
    • 0023034376 scopus 로고
    • Regulatory and cytoskeletal proteins of vertebrate skeletal muscle
    • Ohtsuki I, Maruyama K, and Ebashi S (1986) Regulatory and cytoskeletal proteins of vertebrate skeletal muscle. Adv. Protein Chem. 38: 1-67.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 1-67
    • Ohtsuki, I.1    Maruyama, K.2    Ebashi, S.3
  • 3
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot A S and Potter J D (1987) Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Biophys. Chem. 16: 535-559.
    • (1987) Annu. Rev. Biophys. Biophys. Chem. , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2
  • 4
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah C S and Reinach 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    Reinach, F.C.2
  • 5
    • 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
  • 6
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 A resolution
    • Herzberg O and James M N (1985) Structure of the calcium regulatory muscle protein troponin-C at 2.8 A resolution. Nature 313: 653-659.
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.2
  • 7
    • 0021950702 scopus 로고
    • Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution
    • Sundaralingam M et al. (1985) Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution. Science 227: 945-948.
    • (1985) Science , vol.227 , pp. 945-948
    • Sundaralingam, M.1
  • 8
    • 0032574791 scopus 로고    scopus 로고
    • Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution
    • Vassylyev D G, Takeda S, Wakatsuki S, Maeda K, and Maeda Y (1998) Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution. Proc. Natl. Acad. Sci. USA 95: 4847-4852.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4847-4852
    • Vassylyev, D.G.1    Takeda, S.2    Wakatsuki, S.3    Maeda, K.4    Maeda, Y.5
  • 9
    • 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
  • 10
    • 0017280755 scopus 로고
    • The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit
    • Syska H, Wilkinson J M, Grand R J, and Perry S V (1976) The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Biochem. J. 153: 375-387.
    • (1976) Biochem. J. , vol.153 , pp. 375-387
    • Syska, H.1    Wilkinson, J.M.2    Grand, R.J.3    Perry, S.V.4
  • 11
    • 0019474543 scopus 로고
    • Synthetic studies on the inhibitory region of rabbit skeletal troponin I. Relationship of amino acid sequence to biological activity
    • Talbot J A and Hodges R S (1981) Synthetic studies on the inhibitory region of rabbit skeletal troponin I. Relationship of amino acid sequence to biological activity. J. Biol. Chem. 256: 2798-2802.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2798-2802
    • Talbot, J.A.1    Hodges, R.S.2
  • 12
    • 0028137004 scopus 로고
    • Structural and regulatory functions of the NH2- and COOH-terminal regions of skeletal muscle troponin I
    • Farah C S et al. (1994) Structural and regulatory functions of the NH2- and COOH-terminal regions of skeletal muscle troponin I. J. Biol. Chem. 269: 5230-5240.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5230-5240
    • Farah, C.S.1
  • 13
    • 0033614841 scopus 로고    scopus 로고
    • Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C
    • Li M X, Spyracopoulos L, and Sykes B D (1999) Binding of cardiac troponin-I147-163 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
  • 14
    • 0037588762 scopus 로고    scopus 로고
    • Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form
    • Takeda S, Yamashita A, Maeda K, and Maeda Y (2003) Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. Nature 424: 35-41.
    • (2003) Nature , vol.424 , pp. 35-41
    • Takeda, S.1    Yamashita, A.2    Maeda, K.3    Maeda, Y.4
  • 15
    • 0030952840 scopus 로고    scopus 로고
    • Structural and functional domains of the troponin complex revealed by limited digestion
    • Takeda S, Kobayashi T, Taniguchi H, Hayashi H, and Maeda Y (1997) Structural and functional domains of the troponin complex revealed by limited digestion. Eur. J. Biochem. 246: 611-617.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 611-617
    • Takeda, S.1    Kobayashi, T.2    Taniguchi, H.3    Hayashi, H.4    Maeda, Y.5
  • 16
    • 0026342025 scopus 로고    scopus 로고
    • Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing
    • Weis W I, Kahn R, Fourme R, Drickamer K, and Hendrickson W A, Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science 254: 1608-1615.
    • Science , vol.254 , pp. 1608-1615
    • Weis, W.I.1    Kahn, R.2    Fourme, R.3    Drickamer, K.4    Hendrickson, W.A.5
  • 17
    • 0032477852 scopus 로고    scopus 로고
    • Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: Potential role for coiled coil interaction
    • Stefancsik R, Jha P K, and Sarkar S (1998) Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: potential role for coiled coil interaction. Proc. Natl. Acad. Sci. USA 95: 957-962.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 957-962
    • Stefancsik, R.1    Jha, P.K.2    Sarkar, S.3
  • 18
    • 0031554903 scopus 로고    scopus 로고
    • Mapping of a second actin-tropomyosin and a second troponin C binding site within the C terminus of troponin I, and their importance in the Ca2+-dependent regulation of muscle contraction
    • Tripet B, Van Eyk J E, and Hodges R S (1997) Mapping of a second actin-tropomyosin and a second troponin C binding site within the C terminus of troponin I, and their importance in the Ca2+-dependent regulation of muscle contraction. J. Mol. Biol. 271: 728-750.
    • (1997) J. Mol. Biol. , vol.271 , pp. 728-750
    • Tripet, B.1    Van Eyk, J.E.2    Hodges, R.S.3
  • 19
    • 0000244537 scopus 로고
    • Structural changes in the actin- and myosin-containing filaments during contraction
    • Huxley H E (1972) Structural changes in the actin- and myosin-containing filaments during contraction. Cold Spring harbor Symp. Quant. Biol. 37: 361-376.
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 20
    • 0000733783 scopus 로고
    • X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle
    • Haselgrove J C (1972) X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle. Cold Spring harbor Symp. Quant. Biol. 37: 341-352.
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 341-352
    • Haselgrove, J.C.1
  • 21
    • 0015935349 scopus 로고
    • Structural role of tropomyosin in muscle regulation: Analysis of the x-ray diffraction patterns from relaxed and contracting muscles
    • Parry D A and Squire J M (1973) Structural role of tropomyosin in muscle regulation: analysis of the x-ray diffraction patterns from relaxed and contracting muscles. J. Mol. Biol. 75: 33-55.
    • (1973) J. Mol. Biol. , vol.75 , pp. 33-55
    • Parry, D.A.1    Squire, J.M.2
  • 22
    • 0036213649 scopus 로고    scopus 로고
    • Ca2+- and S1-induced conformational changes of reconstituted skeletal muscle thin filaments observed by fluorescence energy transfer spectroscopy: Structural evidence for three States of thin filament
    • Hai H, Sano K, Maeda K, Maeda Y, and Miki M (2002) Ca2+- and S1-induced conformational changes of reconstituted skeletal muscle thin filaments observed by fluorescence energy transfer spectroscopy: structural evidence for three States of thin filament. J. Biochem. (Tokyo) 131: 407-418.
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 407-418
    • Hai, H.1    Sano, K.2    Maeda, K.3    Maeda, Y.4    Miki, M.5
  • 23
    • 0015527223 scopus 로고
    • Effect of calcium ions on the flexibility of reconstituted thin filaments of muscle studied by quasielastic scattering of laser light
    • Ishiwata S and Fujime S (1972) Effect of calcium ions on the flexibility of reconstituted thin filaments of muscle studied by quasielastic scattering of laser light. J. Mol. Biol. 68: 511-522.
    • (1972) J. Mol. Biol. , vol.68 , pp. 511-522
    • Ishiwata, S.1    Fujime, S.2
  • 24
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • Yanagida T, Nakase M, Nishiyama K, and Oosawa F (1984) Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307: 58-60.
    • (1984) Nature , vol.307 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4
  • 25
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop D F and Geeves M A (1993) Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 65: 693-701.
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 26
    • 0028179144 scopus 로고
    • Ca(2+)-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
    • Lehman W, Craig R, and Vibert P (1994) Ca(2+)-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature 368: 65-67.
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 27
    • 0028902929 scopus 로고    scopus 로고
    • Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy
    • Watkins H et al. Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy. N. Engl. J. Med. 332: 1058-1064.
    • N. Engl. J. Med. , vol.332 , pp. 1058-1064
    • Watkins, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.