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Volumn 398, Issue 6722, 1999, Pages 84-90

Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; PROTEIN TYROSINE KINASE;

EID: 0033522219     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/18050     Document Type: Article
Times cited : (251)

References (30)
  • 1
    • 0031759356 scopus 로고    scopus 로고
    • c-Cbl: A regulator of T cell receptor-mediated signalling
    • Thien, C. B. & Langdon, W. Y. c-Cbl: a regulator of T cell receptor-mediated signalling. Immunol. Cell Biol. 76, 473-482 (1998).
    • (1998) Immunol. Cell Biol. , vol.76 , pp. 473-482
    • Thien, C.B.1    Langdon, W.Y.2
  • 2
    • 0031869038 scopus 로고    scopus 로고
    • Cbl: Complex formation and functional implications
    • Liu, Y. C. & Altman, A. Cbl: Complex formation and functional implications. Cell Signal, 10, 377-385 (1998).
    • (1998) Cell Signal , vol.10 , pp. 377-385
    • Liu, Y.C.1    Altman, A.2
  • 3
    • 0031433275 scopus 로고    scopus 로고
    • The Cbl proto-oncogene product: From enigmatic oncogene to center stage of signal transduction
    • Miyake, S. et al. The Cbl proto-oncogene product: From enigmatic oncogene to center stage of signal transduction. Crit. Rev. Oncogen, 8, 189-218 (1998).
    • (1998) Crit. Rev. Oncogen , vol.8 , pp. 189-218
    • Miyake, S.1
  • 4
    • 0030250114 scopus 로고    scopus 로고
    • Complex complexes: Signaling at the TCR
    • Wange, R. L. & Samelson, L. E. Complex complexes: signaling at the TCR. Immunity 5, 197-205 (1996).
    • (1996) Immunity , vol.5 , pp. 197-205
    • Wange, R.L.1    Samelson, L.E.2
  • 5
    • 0031011155 scopus 로고    scopus 로고
    • EGF receptor binding and transformation by v-cbl is ablated by the introduction of a loss-of-function mutation from the Caenorhabditis elegans sli-1 gene
    • Thien, C. B. & Langdon, W. Y. EGF receptor binding and transformation by v-cbl is ablated by the introduction of a loss-of-function mutation from the Caenorhabditis elegans sli-1 gene. Oncogene 14, 2239-2249 (1997).
    • (1997) Oncogene , vol.14 , pp. 2239-2249
    • Thien, C.B.1    Langdon, W.Y.2
  • 6
    • 14444276991 scopus 로고    scopus 로고
    • The Cbl phospholyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70
    • Lupher, M. L. Jr, Songyang, Z., Shoelson, S. E., Cantley, L. C. & Band, H. The Cbl phospholyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70. J. Biol. Chem. 272, 33140-33144 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 33140-33144
    • Lupher M.L., Jr.1    Songyang, Z.2    Shoelson, S.E.3    Cantley, L.C.4    Band, H.5
  • 7
    • 0030032040 scopus 로고    scopus 로고
    • Calcium binding and conformational response in EF-hand proteins
    • Ikura, M. Calcium binding and conformational response in EF-hand proteins. Trends Biochem. Sci. 21, 14-17 (1996).
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 14-17
    • Ikura, M.1
  • 8
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kuriyan, J. & Cowburn, D. Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26, 259-288 (1997).
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 10
    • 0025819499 scopus 로고
    • The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif
    • Blake, T. J., Shapiro, M., Morse, H. C. & Langdon, W. Y. The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif Oncogene 6, 653-657 (1991).
    • (1991) Oncogene , vol.6 , pp. 653-657
    • Blake, T.J.1    Shapiro, M.2    Morse, H.C.3    Langdon, W.Y.4
  • 11
    • 0029094649 scopus 로고
    • Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation
    • Galisteo, M. L., Dikic, I., Batzer, A. G., Langdon, W. Y. & Schlessinger, J. Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation. J. Biol. Chem. 270, 20242-20243 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 20242-20243
    • Galisteo, M.L.1    Dikic, I.2    Batzer, A.G.3    Langdon, W.Y.4    Schlessinger, J.5
  • 12
    • 0032502734 scopus 로고    scopus 로고
    • Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases
    • Deckert, M., Elly, C., Altman, A. & Liu, Y. C. Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases. J. Biol. Chem. 273, 8867-8874 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8867-8874
    • Deckert, M.1    Elly, C.2    Altman, A.3    Liu, Y.C.4
  • 13
    • 0029124883 scopus 로고
    • Similarity of sli-1, a regulator of vulval development in C. Elegans, to the mammalian proto-oncogene c-cbl
    • Yoon, C. H., Lee, J., longeward, G. D. & Sternberg, P. W. Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl. Science 269, 1102-1105 (1995).
    • (1995) Science , vol.269 , pp. 1102-1105
    • Yoon, C.H.1    Lee, J.2    Longeward, G.D.3    Sternberg, P.W.4
  • 14
    • 0030978136 scopus 로고    scopus 로고
    • Interactions of Drosophila Cbl with epidermal growth factor receptors and role of Cbl in R7 photoreceptor cell development
    • Meisner, H. et al. Interactions of Drosophila Cbl with epidermal growth factor receptors and role of Cbl in R7 photoreceptor cell development. Mol. Cell Biol. 17, 2217-2225 (1997).
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2217-2225
    • Meisner, H.1
  • 15
    • 0030889218 scopus 로고    scopus 로고
    • The product of the proto-oncogene c-cbl: A negative regulator of the Syk tyrosine kinase
    • Ota, Y. & Samelson, L. E. The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase. Science 276, 418-420 (1997).
    • (1997) Science , vol.276 , pp. 418-420
    • Ota, Y.1    Samelson, L.E.2
  • 16
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm, L. & Sander, C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20, 478-480 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 18
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • Essen, L. O., Perisic, O., Cheung, R., Katan, M. & Williams, R. L. Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 380, 595-602 (1996).
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 19
    • 0032575695 scopus 로고    scopus 로고
    • Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain
    • de Beer, T., Carter, R. E., Lobel-Rice, K. E., Sorkin, A. & Overduin, M. Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. Science 281, 1357-1360 (1998).
    • (1998) Science , vol.281 , pp. 1357-1360
    • De Beer, T.1    Carter, R.E.2    Lobel-Rice, K.E.3    Sorkin, A.4    Overduin, M.5
  • 20
    • 0032499801 scopus 로고    scopus 로고
    • Three-dimensional structure of the Stat3β homodimer bound to DNA
    • Becker, S., Groner, B. & Muller, C. W. Three-dimensional structure of the Stat3β homodimer bound to DNA. Nature 394, 145-151 (1998).
    • (1998) Nature , vol.394 , pp. 145-151
    • Becker, S.1    Groner, B.2    Muller, C.W.3
  • 21
    • 0032577678 scopus 로고    scopus 로고
    • Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA
    • Chen, X. et al. Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Cell 93, 827-839 (1998).
    • (1998) Cell , vol.93 , pp. 827-839
    • Chen, X.1
  • 22
    • 84988043558 scopus 로고
    • Molecular basis for the interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor
    • Hatada, M. H. et al. Molecular basis for the interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor. Nature 377, 32-38 (1995).
    • (1995) Nature , vol.377 , pp. 32-38
    • Hatada, M.H.1
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein cryssellograpby
    • Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein cryssellograpby. Acta Crystallogr. D 50, 760-776 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-776
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zhou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.