메뉴 건너뛰기




Volumn 5, Issue 7, 1997, Pages 949-959

Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin

Author keywords

Dynamics; Fibronectin; NMR spectroscopy; RGD motif; Tenascin

Indexed keywords


EID: 0031571127     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00248-7     Document Type: Article
Times cited : (86)

References (49)
  • 1
    • 0025814801 scopus 로고
    • Arginyl-glycylaspartic acid (RGD): A cell adhesion motif
    • D'Souza, S.E., Ginsberg, M.H. & Plow, E.F. (1991). Arginyl-glycylaspartic acid (RGD): a cell adhesion motif. Trends Biochem. Sci. 16, 246-250.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 246-250
    • D'Souza, S.E.1    Ginsberg, M.H.2    Plow, E.F.3
  • 2
    • 0004043397 scopus 로고
    • Springer-Verlag, New York, NY, USA
    • Hynes, R.O. (1990). Fibronectins, Springer-Verlag, New York, NY, USA.
    • (1990) Fibronectins
    • Hynes, R.O.1
  • 3
    • 0026040206 scopus 로고
    • Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using sitedirected mutagenesis
    • Aota, S., Nagai, T. & Yamada, K.M. (1991). Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using sitedirected mutagenesis. J. Biol. Chem. 266, 15938-15943.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15938-15943
    • Aota, S.1    Nagai, T.2    Yamada, K.M.3
  • 4
    • 0027685702 scopus 로고
    • Tenascin-C, tenascin-R and tenascin-X: A family of talented proteins in search of functions
    • Erickson, H.P. (1993). Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions. Curr. Opin. Cell Biol. 5, 869-876.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 869-876
    • Erickson, H.P.1
  • 5
    • 0027497077 scopus 로고
    • Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin
    • Joshi, P., Chung, C.-Y., Aukhil, I. & Erickson, H.P. (1993). Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin. J. Cell Sci. 106, 389-400.
    • (1993) J. Cell Sci. , vol.106 , pp. 389-400
    • Joshi, P.1    Chung, C.-Y.2    Aukhil, I.3    Erickson, H.P.4
  • 6
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain fromtenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy, D.J., Hendrickson, W.A., Aukhil, I. & Erickson, H.P. (1992). Structure of a fibronectin type III domain fromtenascin phased by MAD analysis of the selenomethionyl protein. Science 258, 987-991.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 7
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main, A.L., Harvey, T.S., Baron, M., Boyd, J. & Campbell, I.D. (1992). The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 71, 671-678.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 8
    • 0028216926 scopus 로고
    • Crystal structure of the tenth type III cell adhesion module of human fibronectin
    • Dickinson, C.D., et. al., & Ely, K.R. (1994). Crystal structure of the tenth type III cell adhesion module of human fibronectin. J. Mol. Biol. 236, 1079-1092.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1079-1092
    • Dickinson, C.D.1    Ely, K.R.2
  • 9
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy, D.J., Aukhil, I. & Erickson, H.P. (1996). 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84, 155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 10
    • 0031556949 scopus 로고    scopus 로고
    • Module-module interactions in the cell binding region of fibronectin: Stability, flexibility and specificity
    • Spitzfaden, C., Grant, R.P., Mardon, H.J. & Campbell, I.D. (1997). Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity. J. Mol. Biol. 265, 565-579.
    • (1997) J. Mol. Biol. , vol.265 , pp. 565-579
    • Spitzfaden, C.1    Grant, R.P.2    Mardon, H.J.3    Campbell, I.D.4
  • 11
    • 0026425975 scopus 로고
    • Rusting of the lock and key model for proteinligand binding
    • Jorgensen, W.L. (1991). Rusting of the lock and key model for proteinligand binding. Science 254, 954-955.
    • (1991) Science , vol.254 , pp. 954-955
    • Jorgensen, W.L.1
  • 12
    • 0029331769 scopus 로고
    • High-affinity rat antifluorescein monoclonal antibody with unique fine specificity properties including differential recognition of dynamic ligand analogues
    • Miklasz, S.D., Gulliver, G.A. & Voss, E.W. (1995). High-affinity rat antifluorescein monoclonal antibody with unique fine specificity properties including differential recognition of dynamic ligand analogues. J. Mol. Recog. 8, 258-269.
    • (1995) J. Mol. Recog. , vol.8 , pp. 258-269
    • Miklasz, S.D.1    Gulliver, G.A.2    Voss, E.W.3
  • 13
    • 0030042698 scopus 로고    scopus 로고
    • Correlation between dynamics and high affinity binding in an SH2 domain interaction
    • Kay, L.E., Muhandiram, D.R., Farrow, N.A., Aubin, Y. & Forman-Kay, J.D. (1996). Correlation between dynamics and high affinity binding in an SH2 domain interaction. Biochemistry 35, 361-368.
    • (1996) Biochemistry , vol.35 , pp. 361-368
    • Kay, L.E.1    Muhandiram, D.R.2    Farrow, N.A.3    Aubin, Y.4    Forman-Kay, J.D.5
  • 14
    • 0029067489 scopus 로고
    • Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity
    • Morton, A. & Matthews, B.W. (1995). Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity. Biochemistry 34, 8576-8588.
    • (1995) Biochemistry , vol.34 , pp. 8576-8588
    • Morton, A.1    Matthews, B.W.2
  • 15
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G. & Szabo, A. (1982). Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104, 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 16
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • Brüschweiler, R., Liao, X. & Wright, P.E. (1995). Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science 268, 886-889.
    • (1995) Science , vol.268 , pp. 886-889
    • Brüschweiler, R.1    Liao, X.2    Wright, P.E.3
  • 18
    • 0025046144 scopus 로고
    • Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
    • Clore, G.M., Szabo, A., Bax, A., Kay, L.E., Driscoll, P.C. & Gronenborn, A.M. (1990). Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins. J. Am. Chem. Soc. 112, 4989-4991.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3    Kay, L.E.4    Driscoll, P.C.5    Gronenborn, A.M.6
  • 20
    • 0028541223 scopus 로고
    • A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization
    • Schurr, J.M., Babcock, H.P. & Fujimoto, B.S. (1994). A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization. J. Magn. Reson. 105, 211-224.
    • (1994) J. Magn. Reson. , vol.105 , pp. 211-224
    • Schurr, J.M.1    Babcock, H.P.2    Fujimoto, B.S.3
  • 21
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A.M., Akke, M. & Palmer, A.G. (1995). Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 246, 144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 23
    • 0028997623 scopus 로고
    • Interactions between type III domains in the 110 kDa cell-binding fragment of fibronectin
    • Litvinovich, S.V. & Ingham, K.C. (1995). Interactions between type III domains in the 110 kDa cell-binding fragment of fibronectin. J. Mol. Biol. 248, 611-626.
    • (1995) J. Mol. Biol. , vol.248 , pp. 611-626
    • Litvinovich, S.V.1    Ingham, K.C.2
  • 24
    • 0028920871 scopus 로고
    • Concept and progress in the development of RGD-containing peptide pharmaceuticals
    • Craig, W.S., Cheng, S., Mullen, D.G., Blevitt, J. & Pierschbacher, M.D. (1995). Concept and progress in the development of RGD-containing peptide pharmaceuticals. Biopolymers 37, 157-175.
    • (1995) Biopolymers , vol.37 , pp. 157-175
    • Craig, W.S.1    Cheng, S.2    Mullen, D.G.3    Blevitt, J.4    Pierschbacher, M.D.5
  • 25
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • Piersbacher, M.D. & Ruoslahti, E. (1987). Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. 262, 17294-17298.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17294-17298
    • Piersbacher, M.D.1    Ruoslahti, E.2
  • 26
    • 0027997413 scopus 로고
    • Selective recognition of cyclic RGD peptides of NMR defined conformation by • llb • 3, • V• 3, and • 5• 1 integrins
    • Pfaff, M., et. al., & Engel, J. (1994). Selective recognition of cyclic RGD peptides of NMR defined conformation by • llb • 3, • V• 3, and • 5• 1 integrins. J. Biol. Chem. 269, 20233-20238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20233-20238
    • Pfaff, M.1    Engel, J.2
  • 27
    • 0027217436 scopus 로고
    • Determination of the nuclear-magnetic-resonance solution structure of cardiotoxin CTX lib from Naja mossambica mossambica
    • O'Connell, J.F., Bougis, P.E. & Wüthrich, K. (1993). Determination of the nuclear-magnetic-resonance solution structure of cardiotoxin CTX lib from Naja mossambica mossambica. Eur. J. Biochem. 213, 891-900.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 891-900
    • O'Connell, J.F.1    Bougis, P.E.2    Wüthrich, K.3
  • 28
    • 0028169737 scopus 로고
    • Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor
    • Fairbrother, W.J., McDowell, R.S. & Cunningham, B.C. (1994). Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor. Biochemistry 33, 8897-8904.
    • (1994) Biochemistry , vol.33 , pp. 8897-8904
    • Fairbrother, W.J.1    McDowell, R.S.2    Cunningham, B.C.3
  • 29
    • 0027995549 scopus 로고
    • LFA-1 binding site in ICAM-3 contains a conserved motif and non-contiguous amino acids
    • Sadhu, C., et. al., & Staunton, D.E. (1994). LFA-1 binding site in ICAM-3 contains a conserved motif and non-contiguous amino acids. Cell Adhes. Commun. 2, 429-440.
    • (1994) Cell Adhes. Commun. , vol.2 , pp. 429-440
    • Sadhu, C.1    Staunton, D.E.2
  • 30
    • 0027474006 scopus 로고
    • Cell- and heparinbinding domains of the hexabrachion arm identified bytenascin expression proteins
    • Aukhil, I., Joshi, P., Yan, Y. & Erickson, H.P. (1993). Cell- and heparinbinding domains of the hexabrachion arm identified bytenascin expression proteins. J. Biol. Chem. 268, 2542-2553.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2542-2553
    • Aukhil, I.1    Joshi, P.2    Yan, Y.3    Erickson, H.P.4
  • 32
    • 0001250026 scopus 로고
    • 1H 2D NMR Spectra by interactive computer graphics
    • 1H 2D NMR Spectra by interactive computer graphics. J. Magn. Reson. 84, 627-633.
    • (1989) J. Magn. Reson. , vol.84 , pp. 627-633
    • Kraulis, P.J.1
  • 33
    • 0028204451 scopus 로고
    • Solution structure and dynamics of ras p21 .GDP determined by heteronuclear three-and four-dimensional NMR spectroscopy
    • Kraulis, P.J., Domaille, P.J., Campbell-Burk, S.L., Van Aken, T. & Laue, E.D. (1994). Solution structure and dynamics of ras p21 .GDP determined by heteronuclear three-and four-dimensional NMR spectroscopy. Biochemistry 33, 3515-3531.
    • (1994) Biochemistry , vol.33 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 34
    • 0026609796 scopus 로고
    • 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin
    • Baron, M., Main, A.L., Driscoll, P.C., Mardon, H.J., Boyd, J. & Campbell, I.D. (1992). 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. Biochemistry 31, 2068-2073.
    • (1992) Biochemistry , vol.31 , pp. 2068-2073
    • Baron, M.1    Main, A.L.2    Driscoll, P.C.3    Mardon, H.J.4    Boyd, J.5    Campbell, I.D.6
  • 36
    • 36849104960 scopus 로고
    • Measurement of spin relaxation in complex systems
    • Void, R.L., Waugh, J.S., Klein, M.P. & Phelps, D.E. (1968). Measurement of spin relaxation in complex systems. J. Chem. Phys. 48, 3831-3832.
    • (1968) J. Chem. Phys. , vol.48 , pp. 3831-3832
    • Void, R.L.1    Waugh, J.S.2    Klein, M.P.3    Phelps, D.E.4
  • 37
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear spin relaxation times
    • Meiboom, S. & Gill, D. (1958). Modified spin-echo method for measuring nuclear spin relaxation times. Rev. Sci. Instrum. 29, 688-691.
    • (1958) Rev. Sci. Instrum. , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 41
    • 0001107873 scopus 로고
    • Improved algorithm for noniterative time-domain model fitting to exponentially damped magnetic resonance signals
    • Barkhuijsen, H., de Beer, R. & van Ormondt, D. (1987). Improved algorithm for noniterative time-domain model fitting to exponentially damped magnetic resonance signals. J. Magn. Reson. 73, 553-557.
    • (1987) J. Magn. Reson. , vol.73 , pp. 553-557
    • Barkhuijsen, H.1    De Beer, R.2    Van Ormondt, D.3
  • 43
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka, A.J., Barker, P.B. & 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
  • 46
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari, G. & Szabo, A. (1982). Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104, 4559-4570.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 47
    • 36849140579 scopus 로고
    • Spin echoes and chemical exchange
    • Bloom, M., Reeves, L.W. & Wells, E.J. (1965). Spin echoes and chemical exchange. J. Chem. Phys. 42, 1615-1624.
    • (1965) J. Chem. Phys. , vol.42 , pp. 1615-1624
    • Bloom, M.1    Reeves, L.W.2    Wells, E.J.3
  • 49
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.