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Volumn 33, Issue 3, 1998, Pages 396-407

Molecular dynamics simulations of epidermal growth factor and transforming growth factor-α structures in water

Author keywords

AMBER; Conformation; Domain movement; Epidermal growth factor; Receptor binding; Transforming growth factor alpha; Weakly polar interaction

Indexed keywords

EPIDERMAL GROWTH FACTOR; GAMMA UROGASTRONE; TRANSFORMING GROWTH FACTOR ALPHA;

EID: 0032533398     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19981115)33:3<396::AID-PROT8>3.0.CO;2-I     Document Type: Article
Times cited : (6)

References (31)
  • 1
    • 0028618937 scopus 로고
    • Structure-function relationships for the EGF/TGF-α family of mitogens
    • Groenen, L.C., Nice, E.C., Burgess, A.W. Structure-function relationships for the EGF/TGF-α family of mitogens. Growth Factors 11:235-257, 1994.
    • (1994) Growth Factors , vol.11 , pp. 235-257
    • Groenen, L.C.1    Nice, E.C.2    Burgess, A.W.3
  • 2
    • 0018236378 scopus 로고
    • Epidermal growth factor stimulates phosphorylation in membrane preparations in vitro
    • Carpenter, G., Cohen, S. Epidermal growth factor stimulates phosphorylation in membrane preparations in vitro. Nature 276:409-410, 1978.
    • (1978) Nature , vol.276 , pp. 409-410
    • Carpenter, G.1    Cohen, S.2
  • 4
    • 0024357975 scopus 로고
    • Epidermal growth factor promotes chick embryonic angiogenesis
    • Stewart, R., Nelson, J., Wilson, D.J. Epidermal growth factor promotes chick embryonic angiogenesis. Cell. Biol. Int. Rep. 13:957-965, 1989.
    • (1989) Cell. Biol. Int. Rep. , vol.13 , pp. 957-965
    • Stewart, R.1    Nelson, J.2    Wilson, D.J.3
  • 5
    • 0027219558 scopus 로고
    • Growth factors and wound healing: Biochemical properties of growth factors and their receptors
    • Bennet, N.T., Schultz, G.S. Growth factors and wound healing: Biochemical properties of growth factors and their receptors. Am. J. Surg. 165:728-737, 1993.
    • (1993) Am. J. Surg. , vol.165 , pp. 728-737
    • Bennet, N.T.1    Schultz, G.S.2
  • 6
    • 0027214407 scopus 로고
    • Growth factors and wound healing: Part II. Role in normal and chronic wound healing
    • Bennet, N.T., Schultz, G.S. Growth factors and wound healing: Part II. Role in normal and chronic wound healing. Am. J. Surg. 166:75-81, 1993.
    • (1993) Am. J. Surg. , vol.166 , pp. 75-81
    • Bennet, N.T.1    Schultz, G.S.2
  • 7
    • 0023807364 scopus 로고
    • Transforming growth factor α
    • Derynck, R. Transforming growth factor α. Cell 42:593-595, 1988.
    • (1988) Cell , vol.42 , pp. 593-595
    • Derynck, R.1
  • 8
    • 0026980157 scopus 로고
    • A model system for tumor angiogenesis: Involvement of transforming growth factor-α in tube formation of human microvascular endothelial cells induced by esophageal cancer cells
    • Okamura, K., Morimoto, A., Hamanaka, R., et al. A model system for tumor angiogenesis: Involvement of transforming growth factor-α in tube formation of human microvascular endothelial cells induced by esophageal cancer cells. Biochem. Biophys. Res. Commun. 186:1471-1479, 1992.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1471-1479
    • Okamura, K.1    Morimoto, A.2    Hamanaka, R.3
  • 9
    • 0024324505 scopus 로고
    • Epidermal growth factor and transforming growth factor α bind differently to the epidermal growth factor receptor
    • Winkler, M.E., O'Connor, L., Winget, M., Fendly, B. Epidermal growth factor and transforming growth factor α bind differently to the epidermal growth factor receptor. Biochemistry 28:6373-6378, 1989.
    • (1989) Biochemistry , vol.28 , pp. 6373-6378
    • Winkler, M.E.1    O'Connor, L.2    Winget, M.3    Fendly, B.4
  • 10
    • 0028245026 scopus 로고
    • Identification of the high affinity binding site of transforming growth factor-α (TGF-α) for the chicken epidermal growth factor (EGF) receptor using EGF/TGF-α chimeras
    • Kramer, R.H., Lenferink, A.E.G., van Bueren-Koornneef, I.L., van der Meer, A., van de Poll, M.L.M., van Zoelen, E.J.J. Identification of the high affinity binding site of transforming growth factor-α (TGF-α) for the chicken epidermal growth factor (EGF) receptor using EGF/TGF-α chimeras. J. Biol. Chem. 269:8708-8711, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8708-8711
    • Kramer, R.H.1    Lenferink, A.E.G.2    Van Bueren-Koornneef, I.L.3    Van Der Meer, A.4    Van De Poll, M.L.M.5    Van Zoelen, E.J.J.6
  • 11
    • 0015502174 scopus 로고
    • Epidermal growth factor. Location ofdisulfide bonds
    • Savage, C.R. Jr., Hash, J.H., Cohen, S. Epidermal growth factor. Location ofdisulfide bonds. J. Biol. Chem. 247:7612-7621, 1973.
    • (1973) J. Biol. Chem. , vol.247 , pp. 7612-7621
    • Savage Jr., C.R.1    Hash, J.H.2    Cohen, S.3
  • 12
    • 0026544175 scopus 로고
    • Structure of epidermal growth factor bound to perdeuterated dodecylphosphocholine micelles determined by two-dimensional NMR and simulated annealing calculations
    • Kohda, D., Inagaki, F. Structure of epidermal growth factor bound to perdeuterated dodecylphosphocholine micelles determined by two-dimensional NMR and simulated annealing calculations. Biochemistry 31:677-685, 1992.
    • (1992) Biochemistry , vol.31 , pp. 677-685
    • Kohda, D.1    Inagaki, F.2
  • 13
    • 0026464730 scopus 로고
    • Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions
    • Kohda, D., Inagaki, F. Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions. Biochemistry 31:11928-11939, 1992.
    • (1992) Biochemistry , vol.31 , pp. 11928-11939
    • Kohda, D.1    Inagaki, F.2
  • 14
    • 0027186150 scopus 로고
    • Normal mode analysis of mouse epidermal growth factor: Characterization of the harmonic motion
    • Ikura, T., Go, N. Normal mode analysis of mouse epidermal growth factor: Characterization of the harmonic motion. Proteins 16:423-436, 1993.
    • (1993) Proteins , vol.16 , pp. 423-436
    • Ikura, T.1    Go, N.2
  • 15
    • 0027308075 scopus 로고
    • Solution structure of human type-α transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints
    • Moy, F.J., Li, Y.-C., Rauenbuehler, P., Winkler, M.E., Scheraga, H.A., Montelione, G.T. Solution structure of human type-α transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints. Biochemistry 32:7334-7353, 1993.
    • (1993) Biochemistry , vol.32 , pp. 7334-7353
    • Moy, F.J.1    Li, Y.-C.2    Rauenbuehler, P.3    Winkler, M.E.4    Scheraga, H.A.5    Montelione, G.T.6
  • 16
    • 0001603162 scopus 로고    scopus 로고
    • Molecular dynamics simulation of EGF and TGF-α: Conformation and receptor binding properties
    • Lovas, S., Murphy, R.F. Molecular dynamics simulation of EGF and TGF-α: Conformation and receptor binding properties. J. Mol. Struct. 398-399: 543-550, 1997.
    • (1997) J. Mol. Struct. , vol.398-399 , pp. 543-550
    • Lovas, S.1    Murphy, R.F.2
  • 17
    • 0027236656 scopus 로고
    • The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor
    • Campion, S.R., Biamonti, C., Montelione, G.T., Niyogi, S.K. The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor. Prot. Eng. 6:651-659, 1993.
    • (1993) Prot. Eng. , vol.6 , pp. 651-659
    • Campion, S.R.1    Biamonti, C.2    Montelione, G.T.3    Niyogi, S.K.4
  • 18
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley, C.A., Petsko, G.A. Aromatic-aromatic interaction: A mechanism of protein structure stabilization. Science 229: 23-29, 1985.
    • (1985) Science , vol.229 , pp. 23-29
    • Burley, C.A.1    Petsko, G.A.2
  • 19
    • 0002586310 scopus 로고
    • 5-enkephalin bound to a model membrane as determined by high-resolution NMR
    • 5-enkephalin bound to a model membrane as determined by high-resolution NMR. Lett. Pept. Sci. 2:59-70, 1995.
    • (1995) Lett. Pept. Sci. , vol.2 , pp. 59-70
    • Watts, C.R.1    Tessmer, M.R.2    Kallick, D.A.3
  • 20
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids and organic molecules
    • Cornell, W.D., Cieplak, P., Bayly, C.I., et al. A second generation force field for the simulation of proteins, nucleic acids and organic molecules. J. Am. Chem. Soc. 117:5179-5197, 1995.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Bayly, C.I.3
  • 21
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.P., Ciccotti, G., Berendsen, H.J.C. Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes. J. Comput. Phys. 23:327-341, 1977.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 25
    • 0006827855 scopus 로고    scopus 로고
    • St. Louis, MO
    • Tripos Inc. "Sybyl Users Manual." St. Louis, MO, 1996.
    • (1996) Sybyl Users Manual
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., Sander, C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637, 1983.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 0017435119 scopus 로고
    • Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP
    • Zimmerman, S.S., Pottle, M.S., Némethy, G., Scheraga, H.A. Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP. Macromolecules 10:1-9, 1970.
    • (1970) Macromolecules , vol.10 , pp. 1-9
    • Zimmerman, S.S.1    Pottle, M.S.2    Némethy, G.3    Scheraga, H.A.4
  • 29
    • 0029920419 scopus 로고    scopus 로고
    • Simulated annealing with restrained molecular dynamics using CONGEN: Energy refinement of the NMR solution structures of epidermal and type-α transforming growth factors
    • Tajero, R., Bassolino-Klimas, D., Bruccoleri, R.E., Montelione, G.T. Simulated annealing with restrained molecular dynamics using CONGEN: Energy refinement of the NMR solution structures of epidermal and type-α transforming growth factors. Protein Sci. 5:578-592, 1996.
    • (1996) Protein Sci. , vol.5 , pp. 578-592
    • Tajero, R.1    Bassolino-Klimas, D.2    Bruccoleri, R.E.3    Montelione, G.T.4
  • 30
    • 0029075795 scopus 로고
    • The essential dynamics of thermolysin: Confirmation of the hinge-bending motion and comparison of simulations in vacuum and water
    • van Aalten, D.M.F., Amadei, A., Linssen, A.B.M., Eijsink, V.G.H., Vriend, G., Berendsen, H.J.C. The essential dynamics of thermolysin: Confirmation of the hinge-bending motion and comparison of simulations in vacuum and water. Proteins 22:45-54, 1995.
    • (1995) Proteins , vol.22 , pp. 45-54
    • Van Aalten, D.M.F.1    Amadei, A.2    Linssen, A.B.M.3    Eijsink, V.G.H.4    Vriend, G.5    Berendsen, H.J.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.