메뉴 건너뛰기




Volumn 4, Issue 1, 1996, Pages 21-32

Structure of the regulatory domain of scallop myosin at 2 Å resolution: Implications for regulation

Author keywords

Ca2+ binding; Myosin; Regulation

Indexed keywords

GALLUS GALLUS; VERTEBRATA; ANIMALIA;

EID: 0029643912     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00006-8     Document Type: Article
Times cited : (196)

References (25)
  • 1
    • 0025338952 scopus 로고
    • Isolation of the regulatory domain of scallop myosin: Role of the essential light chain in calcium binding
    • Kwon, H., et al., & Szent-Györgyi, A.G. (1990). Isolation of the regulatory domain of scallop myosin: role of the essential light chain in calcium binding. Proc. Natl. Acad. Sci. USA 87, 4771-4775.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4771-4775
    • Kwon, H.1    Szent-Györgyi, A.G.2
  • 2
    • 0028211433 scopus 로고
    • Structure of the regulatory domain of scallop myosin at 2.8 Å resolution
    • Xie, X., et al, & Cohen, C. (1994). Structure of the regulatory domain of scallop myosin at 2.8 Å resolution. Nature 368, 306-312.
    • (1994) Nature , vol.368 , pp. 306-312
    • Xie, X.1    Cohen, C.2
  • 4
    • 0028819841 scopus 로고
    • Target sequence recognition by the calmodulin superfamily: Implications from light chain binding to the regulatory domain of scallop myosin
    • Houdusse, A. & Cohen, C. (1995). Target sequence recognition by the calmodulin superfamily: implications from light chain binding to the regulatory domain of scallop myosin. Proc. Natl. Acad. Sci. USA 92, 10644-10697.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10644-10697
    • Houdusse, A.1    Cohen, C.2
  • 5
    • 0027194702 scopus 로고
    • Three dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment, I., et al., & Holden, H.M. (1993). Three dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-58.
    • (1993) Science , vol.261 , pp. 50-58
    • Rayment, I.1    Holden, H.M.2
  • 6
    • 0021881565 scopus 로고
    • Three-dimensional structure of calmodulin
    • Babu, Y.S., et al., & Cook, W.J. (1985). Three-dimensional structure of calmodulin. Nature 315, 37-40.
    • (1985) Nature , vol.315 , pp. 37-40
    • Babu, Y.S.1    Cook, W.J.2
  • 7
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution
    • Herzberg, O. & James, M.N.G. (1985). Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature 313, 653-659.
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.G.2
  • 8
    • 0018800868 scopus 로고
    • Characterization of homologous divalent metal ion binding sites of vertebrate and molluscan myosins using electron paramagnetic resonance spectroscopy
    • Bagshaw, C.R. & Kendrick-Jones, J. (1979). Characterization of homologous divalent metal ion binding sites of vertebrate and molluscan myosins using electron paramagnetic resonance spectroscopy. J. Mol. Biol. 130, 317-336.
    • (1979) J. Mol. Biol. , vol.130 , pp. 317-336
    • Bagshaw, C.R.1    Kendrick-Jones, J.2
  • 11
    • 0001201683 scopus 로고
    • Control of contraction by calcium binding to myosin
    • (Engel, A.G. & FranziniArmstrong, C., eds), McGraw-Hill, New York
    • Szent-Györgyi, A.G. & Chantier, P.D. (1994). Control of contraction by calcium binding to myosin. In Myology. (Engel, A.G. & FranziniArmstrong, C., eds), vol. 2, pp. 506-528, McGraw-Hill, New York.
    • (1994) Myology , vol.2 , pp. 506-528
    • Szent-Györgyi, A.G.1    Chantier, P.D.2
  • 12
    • 0028576992 scopus 로고
    • Regulation of scallop myosin by the regulatory light chain depends on a single glycine residue
    • Jansco, A. & Szent-Györgyi, A.G. (1994). Regulation of scallop myosin by the regulatory light chain depends on a single glycine residue. Proc. Natl. Acad. Sci. USA 91, 8762-8766.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8762-8766
    • Jansco, A.1    Szent-Györgyi, A.G.2
  • 13
    • 0000596916 scopus 로고
    • Towards an understanding of the effects of calcium on protein structure and function
    • Strynadka, N.C.J. & James, M.N.G. (1991). Towards an understanding of the effects of calcium on protein structure and function. Curr. Opin. Struct Biol. 1, 905-914.
    • (1991) Curr. Opin. Struct Biol. , vol.1 , pp. 905-914
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 14
    • 0027934341 scopus 로고
    • Regulation of expressed truncated smooth muscle myosins
    • Trybus, K.M. (1994). Regulation of expressed truncated smooth muscle myosins. J. Biol. Chem. 269, 20819-2082.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20819-22082
    • Trybus, K.M.1
  • 15
    • 0026588964 scopus 로고
    • Helical reconstruction of frozen-hydrated scallop myosin filaments
    • Vibert, P. (1992). Helical reconstruction of frozen-hydrated scallop myosin filaments. J. Mol. Biol. 223, 661-671.
    • (1992) J. Mol. Biol. , vol.223 , pp. 661-671
    • Vibert, P.1
  • 16
    • 0029594551 scopus 로고
    • Three-dimensional reconstruction of thick-filaments from rapidly frozen, freeze-substituted tarantula muscle
    • in press
    • Padron, R., et al., & Craig, R. (1995). Three-dimensional reconstruction of thick-filaments from rapidly frozen, freeze-substituted tarantula muscle. J. Struct. Biol., in press.
    • (1995) J. Struct. Biol.
    • Padron, R.1    Craig, R.2
  • 17
    • 0026035307 scopus 로고
    • A folded (1 OS) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity
    • Ankrett, R.J., Rowe, A.J., Cross, R.A., Kendrick-Jones, J. & Bagshaw, C.R. (1991). A folded (1 OS) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity. J. Mol. Biol. 217, 323-335.
    • (1991) J. Mol. Biol. , vol.217 , pp. 323-335
    • Ankrett, R.J.1    Rowe, A.J.2    Cross, R.A.3    Kendrick-Jones, J.4    Bagshaw, C.R.5
  • 18
    • 85030013762 scopus 로고
    • Structural elements defining the functional difference between skeletal and smooth muscle regulatory light chains
    • Yang, Z. & Sweeney, H.L. (1995). Structural elements defining the functional difference between skeletal and smooth muscle regulatory light chains. Biophys. J. 68, A62.
    • (1995) Biophys. J. , vol.68
    • Yang, Z.1    Sweeney, H.L.2
  • 20
    • 51149210396 scopus 로고
    • Determination of absolute from relative X-ray intensity data
    • Wilson, A.J.C. (1942). Determination of absolute from relative X-ray intensity data. Nature 150, 151 -152.
    • (1942) Nature , vol.150 , pp. 151-152
    • Wilson, A.J.C.1
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the locations of errors in these models
    • Jones, T.A., Zou J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the locations of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 23
    • 0026597444 scopus 로고
    • The free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, AT. (1992). The free R-value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 282-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 282-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati, V. (1952). Traitement statistique des erreurs dans la determination des structures cristallines. Acta Cryst. 5, 802-810,
    • (1952) Acta Cryst. , vol.5 , pp. 802-810
    • Luzzati, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.