메뉴 건너뛰기




Volumn 85, Issue 5, 1996, Pages 695-705

Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN RECEPTOR;

EID: 0030010590     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81236-2     Document Type: Article
Times cited : (270)

References (49)
  • 2
    • 0028568639 scopus 로고
    • A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors
    • Blaikie, P., Immanuel, D., Wu, J., Li, N., Yajnik, V., and Margolis, B. (1994). A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem. 269, 32031-32034.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32031-32034
    • Blaikie, P.1    Immanuel, D.2    Wu, J.3    Li, N.4    Yajnik, V.5    Margolis, B.6
  • 3
    • 0029640799 scopus 로고
    • A phosphotyrosine interaction domain
    • Bork, P., and Margolis, B. (1995). A phosphotyrosine interaction domain. Cell 80, 693-694.
    • (1995) Cell , vol.80 , pp. 693-694
    • Bork, P.1    Margolis, B.2
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994). The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50, 760-776.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-776
  • 11
    • 0030066325 scopus 로고    scopus 로고
    • Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2
    • Eck, M.J., Pluskey, S., Trüb, T., Harrison, S.C., and Shoelson, S.E. (1996). Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2. Nature 379, 277-280.
    • (1996) Nature , vol.379 , pp. 277-280
    • Eck, M.J.1    Pluskey, S.2    Trüb, T.3    Harrison, S.C.4    Shoelson, S.E.5
  • 12
    • 0027945789 scopus 로고
    • Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin
    • Ferguson, K., Lemmon, M., Schlessinger, J., and Sigler, P. (1994). Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin. Cell 79, 199-209.
    • (1994) Cell , vol.79 , pp. 199-209
    • Ferguson, K.1    Lemmon, M.2    Schlessinger, J.3    Sigler, P.4
  • 13
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol triphosphate with a PLC pleckstrin homology domain
    • Ferguson, K.M., Lemmon, M.A., Schlessinger, J., and Sigler, P.B. (1995). Structure of the high affinity complex of inositol triphosphate with a PLC pleckstrin homology domain. Cell 83, 1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 14
    • 0029598484 scopus 로고
    • The regions of the Fe65 protein to the phosphtyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein
    • Fiore, F., Zambrano, N., Minopoli, G., Donini, V., Duilio, A., and Russo, T. (1995). The regions of the Fe65 protein to the phosphtyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein. J. Biol. Chem. 270, 30853-30856.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30853-30856
    • Fiore, F.1    Zambrano, N.2    Minopoli, G.3    Donini, V.4    Duilio, A.5    Russo, T.6
  • 15
    • 0028912999 scopus 로고
    • Phosphotyrosine-dependent interaction of Shc and IRS-1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain
    • Gustafson, T.A., He, W., Craparo, A., Schaub, C.D., and O'Neill, T.J. (1995). Phosphotyrosine-dependent interaction of Shc and IRS-1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol. Cell. Biol. 15, 2500-2508.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2500-2508
    • Gustafson, T.A.1    He, W.2    Craparo, A.3    Schaub, C.D.4    O'Neill, T.J.5
  • 17
    • 0028783488 scopus 로고
    • Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via non-SH2 domains
    • He, W., O'Neill, T.J., and Gustafson, T.A. (1995). Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via non-SH2 domains. J. Biol. Chem. 270, 23258-23262.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23258-23262
    • He, W.1    O'Neill, T.J.2    Gustafson, T.A.3
  • 18
    • 0029898718 scopus 로고    scopus 로고
    • Interaction of insulin receptor substrate-2 with the insulin and IGF-1 receptors: Evidence for two distinct phosphotyrosine-dependent interaction domains within IRS-2
    • He, W., Craparo, A., Zhu, Y., O'Neill, T.J., Wang, L.M., Pierce, J.H., and Gustafson, T.A. (1996). Interaction of insulin receptor substrate-2 with the insulin and IGF-1 receptors: evidence for two distinct phosphotyrosine-dependent interaction domains within IRS-2. J. Biol. Chem. 271, 11641-11645.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11641-11645
    • He, W.1    Craparo, A.2    Zhu, Y.3    O'Neill, T.J.4    Wang, L.M.5    Pierce, J.H.6    Gustafson, T.A.7
  • 19
    • 0028582185 scopus 로고
    • Crystal structure of the tryosine kinase domain of the human insulin receptor
    • Hubbard, S.R., Wei, L., Ellis, L., and Hendrickson, W.A. (1994). Crystal structure of the tryosine 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
  • 22
    • 85046526624 scopus 로고
    • Evaluation of single crystal diffraction data from a position sensitive detector
    • Kabsch, W.J. (1988). Evaluation of single crystal diffraction data from a position sensitive detector. J. Appl. Crystallogr. 21, 916-924.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.J.1
  • 23
    • 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
  • 24
    • 0029067403 scopus 로고
    • PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine
    • Kavanaugh, W.M., Turck, C.W., and Williams, L.T. (1995). PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 268, 1177-1179.
    • (1995) Science , vol.268 , pp. 1177-1179
    • Kavanaugh, W.M.1    Turck, C.W.2    Williams, L.T.3
  • 26
    • 0028773467 scopus 로고
    • Crystal structures of peptide complexes of the N-terminal SH2 domain of the Syp tyrosine phosphatase
    • Lee, C.H., Kominos, D., Jaques, S., Margolis, B., Schlessinger, J., Shoelson, S.E., and Kuriyan, J. (1994). Crystal structures of peptide complexes of the N-terminal SH2 domain of the Syp tyrosine phosphatase. Structure 2, 423-438.
    • (1994) Structure , vol.2 , pp. 423-438
    • Lee, C.H.1    Kominos, D.2    Jaques, S.3    Margolis, B.4    Schlessinger, J.5    Shoelson, S.E.6    Kuriyan, J.7
  • 30
    • 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
  • 31
    • 0029878266 scopus 로고    scopus 로고
    • Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes
    • Nolte, R., Eck, M., Schlessinger, J., Shoelson, S., and Harrison, S. (1996). Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes. Nat. Struct. Biol. 3, 364-373.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 364-373
    • Nolte, R.1    Eck, M.2    Schlessinger, J.3    Shoelson, S.4    Harrison, S.5
  • 32
    • 0027969225 scopus 로고
    • Characterization of an interaction between insulin receptor substrate 1 and the insulin receptor by using the two-hybrid system
    • O'Neill, T.J., Craparo, A., and Gustafson, T.A. (1994). Characterization of an interaction between insulin receptor substrate 1 and the insulin receptor by using the two-hybrid system. Mol. Cell. Biol. 14, 6433-6442.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6433-6442
    • O'Neill, T.J.1    Craparo, A.2    Gustafson, T.A.3
  • 33
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • W. Wolf, P.R. Evans, and A.G.W. Leslie, eds. (Warrington, United Kingdom: Science and Engineering Council/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. (Warrington, United Kingdom: Science and Engineering Council/Daresbury Laboratory), pp. 80-86
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 35
    • 0029866195 scopus 로고    scopus 로고
    • IRS-2 binds to the insulin receptor through its PTB domain and through a newly identified domain comprising amino acids 591-786
    • Sawka-Verheile, D., Tartare-Deckert, S., White, M.F., and Van Obberghen, E. (1996). IRS-2 binds to the insulin receptor through its PTB domain and through a newly identified domain comprising amino acids 591-786. J. Biol. Chem. 271, 5980-5983.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5980-5983
    • Sawka-Verheile, D.1    Tartare-Deckert, S.2    White, M.F.3    Van Obberghen, E.4
  • 37
    • 0027437376 scopus 로고
    • Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1
    • Sun, X.J., Crimmins, D.L., Myers, M.G., Jr., Miralpeix, M., and White, M.F. (1993). Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1. Mol. Cell. Biol. 13, 7418-7428.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7418-7428
    • Sun, X.J.1    Crimmins, D.L.2    Myers M.G., Jr.3    Miralpeix, M.4    White, M.F.5
  • 39
    • 0002016798 scopus 로고
    • Isomorphous replacement: Effects of errors on the phase probability distribution
    • Terwilliger, T.C., and Eisenberg, D. (1988). Isomorphous replacement: effects of errors on the phase probability distribution. Acta Crystallogr. A43, 6-13.
    • (1988) Acta Crystallogr. , vol.A43 , pp. 6-13
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 40
    • 0029094991 scopus 로고
    • Specificity of the PTB domain of Shc for β turn-forming pentapeptide motifs amino-terminal to phosphotyrosine
    • Trüb, T., Choi, W.E., Wolf, G., Ottinger, E., Chen, Y., Weiss, M.A., and Shoelson, S.E. (1995). Specificity of the PTB domain of Shc for β turn-forming pentapeptide motifs amino-terminal to phosphotyrosine. J. Biol. Chem. 270, 18205-18208.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18205-18208
    • Trüb, T.1    Choi, W.E.2    Wolf, G.3    Ottinger, E.4    Chen, Y.5    Weiss, M.A.6    Shoelson, S.E.7
  • 42
    • 0029029892 scopus 로고
    • Tyrosine phosphorylation of insulin receptor substrate-1 in vivo depends upon the presence of its pleckstrin homology region
    • Voliovitch, H., Schindler, D.G., Hadari, Y.R., Taylor, S.I., Accili, D., and Zick, Y. (1995). Tyrosine phosphorylation of insulin receptor substrate-1 in vivo depends upon the presence of its pleckstrin homology region. J. Biol. Chem. 270, 18083-18087.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18083-18087
    • Voliovitch, H.1    Schindler, D.G.2    Hadari, Y.R.3    Taylor, S.I.4    Accili, D.5    Zick, Y.6
  • 44
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman, G., Shoelson, S.E., Pant, N., Cowburn, D., and Kuriyan, J. (1993). Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72, 779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 45
    • 0023814924 scopus 로고
    • Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect tyrosine kinase activity
    • White, M.F., Livingston, J.N., Backer, J.M., Lauris, V., Dull, T.J., Ullrich, A., and Kahn, C.R. (1988a). Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect tyrosine kinase activity. Cell 54, 641-649.
    • (1988) Cell , vol.54 , pp. 641-649
    • White, M.F.1    Livingston, J.N.2    Backer, J.M.3    Lauris, V.4    Dull, T.J.5    Ullrich, A.6    Kahn, C.R.7
  • 46
    • 0023834406 scopus 로고
    • A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor
    • White, M.F., Shoelson, S.E., Keutmann, H., and Kahn, C.R. (1988b). A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor. J. Biol. Chem. 263, 2969-2980.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2969-2980
    • White, M.F.1    Shoelson, S.E.2    Keutmann, H.3    Kahn, C.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.