메뉴 건너뛰기




Volumn 86, Issue 4, 1996, Pages 577-587

Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; FIBROBLAST GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 0030598848     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80131-2     Document Type: Article
Times cited : (339)

References (37)
  • 1
    • 0026736833 scopus 로고
    • The FGF family of growth factors and oncogenes
    • Basilico, C., and Moscatelli, D. (1992). The FGF family of growth factors and oncogenes. Adv. Cancer Res. 59, 115-165.
    • (1992) Adv. Cancer Res. , vol.59 , pp. 115-165
    • Basilico, C.1    Moscatelli, D.2
  • 4
    • 0343069451 scopus 로고
    • New Haven, Connecticut: The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University
    • Brünger, A.T. (1992). X-PLOR (Version 3.1) Manual (New Haven, Connecticut: The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University).
    • (1992) X-PLOR (Version 3.1) Manual
    • Brünger, A.T.1
  • 6
    • 0026240806 scopus 로고
    • Ribbons 2.0
    • Carson, M. (1991). Ribbons 2.0. J. Appl. Cryst. 24, 958-961.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 958-961
    • Carson, M.1
  • 8
    • 0028786671 scopus 로고
    • An FGF receptor signaling pathway is required for the normal cell migrations of the sex myoblasts in C. elegans hermaphrodites
    • DeVore, D.L., Horvitz, H.R., and Stern, M.J. (1995). An FGF receptor signaling pathway is required for the normal cell migrations of the sex myoblasts in C. elegans hermaphrodites. Cell 83, 611-620.
    • (1995) Cell , vol.83 , pp. 611-620
    • DeVore, D.L.1    Horvitz, H.R.2    Stern, M.J.3
  • 9
    • 0022494971 scopus 로고
    • Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
    • Ellis, L., Clauser, E., Morgan, D.O., Edery, M., Roth, R.A.,and Rutter, W.J. (1986). Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45, 721-732.
    • (1986) Cell , vol.45 , pp. 721-732
    • Ellis, L.1    Clauser, E.2    Morgan, D.O.3    Edery, M.4    Roth, R.A.5    Rutter, W.J.6
  • 10
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 11
    • 0000933280 scopus 로고
    • Transformations to optimize the superposition of similar structures
    • Hendrickson, W.A. (1979). Transformations to optimize the superposition of similar structures. Acta Cryst. A35, 158-163.
    • (1979) Acta Cryst. , vol.A35 , pp. 158-163
    • Hendrickson, W.A.1
  • 12
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard, S.R., Wei, L., Ellis, L., and Hendrickson, W.A. (1994). Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature. 372, 746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 13
    • 0025123333 scopus 로고
    • The structure of protein - Protein recognition sites
    • Janin, J., and Chothia, C. (1990). The structure of protein - protein recognition sites. J. Biol. Chem. 265, 16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 14
    • 0026649742 scopus 로고
    • Fibroblast growth factor receptor tyrosine kinases: Molecular analysis and signal transduction
    • Jaye, M., Schlessinger, J., and Dionne, C.A. (1992). Fibroblast growth factor receptor tyrosine kinases: molecular analysis and signal transduction. Biochem. Biophys. Acta 1135, 185-199.
    • (1992) Biochem. Biophys. Acta , vol.1135 , pp. 185-199
    • Jaye, M.1    Schlessinger, J.2    Dionne, C.A.3
  • 15
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L.N., Noble, M.E.M., and Owen, D.J. (1996). Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 16
    • 0022333120 scopus 로고
    • Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO
    • Jones, T.A. (1985). Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO. Methods Enzymol. 115, 157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 17
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 18
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
    • Kavanaugh, W.M., and Williams, L.T. (1994). An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266, 1862-1865.
    • (1994) Science , vol.266 , pp. 1862-1865
    • Kavanaugh, W.M.1    Williams, L.T.2
  • 19
    • 0026759727 scopus 로고
    • Breathless, a Drosophila FGF receptor homolog, is essential for migration of tracheal and specific midline glial cells
    • Klambt, C., Glazer, L., and Shilo, B.C. (1992). Breathless, a Drosophila FGF receptor homolog, is essential for migration of tracheal and specific midline glial cells. Genes Dev. 6, 1668-1678.
    • (1992) Genes Dev. , vol.6 , pp. 1668-1678
    • Klambt, C.1    Glazer, L.2    Shilo, B.C.3
  • 20
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R., Zheng, J., Ten Eyck, L.F., Ashford, V.A., Xuong, N.-H., Taylor, S.S., and Sowadski, J.M. (1991). Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414.
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 0026641249 scopus 로고
    • Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis
    • Mohammadi, M., Dionne, C.A., Li, W., Li, N., Spivak, T., Honegger, A.M., Jaye, M., and Schlessinger, J. (1992). Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis. Nature 358, 681-684.
    • (1992) Nature , vol.358 , pp. 681-684
    • Mohammadi, M.1    Dionne, C.A.2    Li, W.3    Li, N.4    Spivak, T.5    Honegger, A.M.6    Jaye, M.7    Schlessinger, J.8
  • 24
    • 0030027488 scopus 로고    scopus 로고
    • Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction
    • Mohammadi, M., Dikic, I., Sorokin, A., Burgess, W.H., Jaye, M., and Schlessinger, J. (1996). Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction. Mol. Cell. Biol. 16, 977-989.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 977-989
    • Mohammadi, M.1    Dikic, I.2    Sorokin, A.3    Burgess, W.H.4    Jaye, M.5    Schlessinger, J.6
  • 25
    • 0029935895 scopus 로고    scopus 로고
    • Graded activation of fibroblast growth factor receptors by mutations causing achondroplasiaand thanatophoric dysplasia
    • Naski, M.C., Wang, Q., Xu, J., Ornitz, D.M., (1996). Graded activation of fibroblast growth factor receptors by mutations causing achondroplasiaand thanatophoric dysplasia. Nature Genet. 13, 233-237.
    • (1996) Nature Genet. , vol.13 , pp. 233-237
    • Naski, M.C.1    Wang, Q.2    Xu, J.3    Ornitz, D.M.4
  • 26
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50, 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 27
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 28
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • W. Wolf, P.R. Evans, and A.G.W. Leslie, eds. (Daresbury, United Kingdom: Daresbury Laboratory)
    • Otwinowski, Z. (1991). Maximum likelihood refinement of heavy atom parameters. In Isomorphous Replacement and Anomalous Scattering, W. Wolf, P.R. Evans, and A.G.W. Leslie, eds. (Daresbury, United Kingdom: Daresbury Laboratory), pp. 80-86.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 29
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, and S. Burley, eds. (Daresbury, United Kingdom: SERC Daresbury Laboratory)
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend, L. Sawyer, N. Isaacs, and S. Burley, eds. (Daresbury, United Kingdom: SERC Daresbury Laboratory), pp. 56-62.
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 32
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?
    • Schlessinger, J., Lax, I., and Lemmon, M. (1995). Regulation of growth factor activation by proteoglycans: what is the role of the low affinity receptors? Cell 83, 357-360.
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlessinger, J.1    Lax, I.2    Lemmon, M.3
  • 34
    • 0028818886 scopus 로고
    • How do protein kinases discriminate between serine/threonine and tyrosine? stuctural insights from the insulin receptor protein-tyrosine kinase
    • Taylor, S.S., Radzio-Andzelm, E., and Hunter, T. (1995). How do protein kinases discriminate between serine/threonine and tyrosine? Stuctural insights from the insulin receptor protein-tyrosine kinase. FASEB J. 9, 1255-1266.
    • (1995) FASEB J. , vol.9 , pp. 1255-1266
    • Taylor, S.S.1    Radzio-Andzelm, E.2    Hunter, T.3
  • 35
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A., and Schlessinger, J. (1990). Signal transduction by receptors with tyrosine kinase activity. Cell 61, 203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 36
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution
    • Zhang, F., Strand, A., Robbins, D., Cobb, M.H., and Goldsmith, E.J. (1994). Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367, 704-711.
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 37
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • Zheng, J., Knighton, D.R., Ten Eyck, L.F., Karlsson, R.K., Xuong, N.-H., Taylor, S.S., and Sowadski, J.M. (1993). Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochem. 32, 2154-2161.
    • (1993) Biochem. , vol.32 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    Ten Eyck, L.F.3    Karlsson, R.K.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.