메뉴 건너뛰기




Volumn 396, Issue 6710, 1998, Pages 486-491

Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; TYROSINE KINASE RECEPTOR;

EID: 0032480889     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/24904     Document Type: Article
Times cited : (96)

References (30)
  • 1
    • 0031559401 scopus 로고    scopus 로고
    • Unified nomenclature for Eph family receptors and their liganda, the ephrins
    • Eph Nomenclature Committee. Unified nomenclature for Eph family receptors and their liganda, the ephrins. Cell 90, 403-440 (1997).
    • (1997) Cell , vol.90 , pp. 403-440
  • 2
    • 0031922119 scopus 로고    scopus 로고
    • The ephrins and Eph receptors in neural development
    • Flanagan, J. G. & Vanderhaeghen, P. The ephrins and Eph receptors in neural development. Annu. Rev. Neurosci. 21, 309-345 (1998).
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 309-345
    • Flanagan, J.G.1    Vanderhaeghen, P.2
  • 3
    • 0029082312 scopus 로고
    • In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases
    • Drescher, U. et al. In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases. Cell 82, 359-370 (1995).
    • (1995) Cell , vol.82 , pp. 359-370
    • Drescher, U.1
  • 4
    • 0344816258 scopus 로고    scopus 로고
    • Nuk controls pathfinding of commissural axons in the mammalian central nervous system
    • Henkemeyer, M. et al. Nuk controls pathfinding of commissural axons in the mammalian central nervous system. Cell 86, 35-46 (1996).
    • (1996) Cell , vol.86 , pp. 35-46
    • Henkemeyer, M.1
  • 5
    • 0029858435 scopus 로고    scopus 로고
    • Sek4 and Nuk receptors cooperate in guidance of commissural axons and in palate formation
    • Orioli, D., Henkemeyer, M., Lemke, G., Klein, R. & Pawson, T. Sek4 and Nuk receptors cooperate in guidance of commissural axons and in palate formation. EMBO J. 15, 6035-6049 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6035-6049
    • Orioli, D.1    Henkemeyer, M.2    Lemke, G.3    Klein, R.4    Pawson, T.5
  • 6
    • 0030957996 scopus 로고    scopus 로고
    • Aberrant axonal projections in mice lacking EphA8 (Eek) tyrosine protein receptors
    • Park, S., Frisen, J. & Barbacid, M. Aberrant axonal projections in mice lacking EphA8 (Eek) tyrosine protein receptors. EMBO J. 16, 3106-3114 (1997).
    • (1997) EMBO J. , vol.16 , pp. 3106-3114
    • Park, S.1    Frisen, J.2    Barbacid, M.3
  • 7
    • 0028989595 scopus 로고
    • Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation
    • Winslow, J. W. et al. Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation. Neuron 14, 973-981 (1995).
    • (1995) Neuron , vol.14 , pp. 973-981
    • Winslow, J.W.1
  • 8
    • 0031213749 scopus 로고    scopus 로고
    • The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted migration of branchial neural crest cells
    • Smith, A., Robinson, V., Patel, K. & Wilkinson, D. G. The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted migration of branchial neural crest cells. Curr. Biol. 7, 561-570 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 561-570
    • Smith, A.1    Robinson, V.2    Patel, K.3    Wilkinson, D.G.4
  • 9
    • 13344261393 scopus 로고
    • Expression of truncated Sek-1 receptor tyrosine kinase disrupts the segmental restriction of gene expression in the Xenopus and zebrafish hindbrain
    • Xu, Q., Alldus, G., Holder, N. & Wilkinson, D. G. Expression of truncated Sek-1 receptor tyrosine kinase disrupts the segmental restriction of gene expression in the Xenopus and zebrafish hindbrain. Development 121, 4005-4016 (1995).
    • (1995) Development , vol.121 , pp. 4005-4016
    • Xu, Q.1    Alldus, G.2    Holder, N.3    Wilkinson, D.G.4
  • 10
    • 0030890656 scopus 로고    scopus 로고
    • Eph family transmembrane ligands can mediate repulsive guidance of trunk neural crest migration and motor axon outgrowth
    • Wang, H. U. & Anderson, D. J. Eph family transmembrane ligands can mediate repulsive guidance of trunk neural crest migration and motor axon outgrowth. Neuron 18, 383-396 (1997).
    • (1997) Neuron , vol.18 , pp. 383-396
    • Wang, H.U.1    Anderson, D.J.2
  • 11
    • 0031214537 scopus 로고    scopus 로고
    • Interactions of Eph-related receptors and ligands confer rostrocaudal pattern to trunk neural crest migration
    • Krull, C. E. et al. Interactions of Eph-related receptors and ligands confer rostrocaudal pattern to trunk neural crest migration. Curr. Biol. 7, 571-580 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 571-580
    • Krull, C.E.1
  • 12
    • 15844429889 scopus 로고    scopus 로고
    • Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis
    • Gale, N. W. et al. Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. Neuron 17, 9-19 (1996).
    • (1996) Neuron , vol.17 , pp. 9-19
    • Gale, N.W.1
  • 13
    • 0029851690 scopus 로고    scopus 로고
    • Bi-directional signalling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland, S. J. et al. Bi-directional signalling through the EPH-family receptor Nuk and its transmembrane ligands. Nature 383, 722-725 (1996).
    • (1996) Nature , vol.383 , pp. 722-725
    • Holland, S.J.1
  • 14
    • 0030891962 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of transmembrane ligands for Eph receptors
    • Bruckner, K., Pasquale, E. B. & Klein, R. Tyrosine phosphorylation of transmembrane ligands for Eph receptors. Science 275, 1640-1643 (1997).
    • (1997) Science , vol.275 , pp. 1640-1643
    • Bruckner, K.1    Pasquale, E.B.2    Klein, R.3
  • 15
    • 0028349863 scopus 로고
    • Immunolocalization of the Nuk receptor tyrosine kinase suggests roles in segmental patterning of the brain and axonogenesis
    • Henkemeyer, M. et al. Immunolocalization of the Nuk receptor tyrosine kinase suggests roles in segmental patterning of the brain and axonogenesis. Oncogene 9, 1001-1014 (1994).
    • (1994) Oncogene , vol.9 , pp. 1001-1014
    • Henkemeyer, M.1
  • 16
    • 0030962317 scopus 로고    scopus 로고
    • The N-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling
    • Labrador, J. P., Brambilla, R. & Klein, R. The N-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling. EMBO J. 16, 3889-3897 (1997).
    • (1997) EMBO J. , vol.16 , pp. 3889-3897
    • Labrador, J.P.1    Brambilla, R.2    Klein, R.3
  • 17
    • 0032493828 scopus 로고    scopus 로고
    • Distinct subdomains of the EphA3 receptor mediate ligand binding and receptor dimerization
    • Lackmann, M. et al. Distinct subdomains of the EphA3 receptor mediate ligand binding and receptor dimerization. J. Biol. Chem. 273, 20228-20237 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 20228-20237
    • Lackmann, M.1
  • 18
    • 0032489430 scopus 로고    scopus 로고
    • The VAB-1 Eph receptor tyrosine kinase functions in neural and epithelial morphogenesis in C. elegans
    • George, S. E., Simokat, K., Hardin, J. & Chisholm, A. D. The VAB-1 Eph receptor tyrosine kinase functions in neural and epithelial morphogenesis in C. elegans. Cell 92, 633-643 (1998).
    • (1998) Cell , vol.92 , pp. 633-643
    • George, S.E.1    Simokat, K.2    Hardin, J.3    Chisholm, A.D.4
  • 19
    • 0030923341 scopus 로고    scopus 로고
    • Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor
    • Lackmann, M. et al. Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor. J. Biol. Chem. 272, 16521-16530 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 16521-16530
    • Lackmann, M.1
  • 21
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm, L. & Sander, C. Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 26, 316-319 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 22
    • 0028170817 scopus 로고
    • Receptor protein-tyrosine kinases and their signal transduction pathways
    • Van der Geer, P., Hunter, T. & Lindberg, R. A. Receptor protein-tyrosine kinases and their signal transduction pathways. Annu. Rev. Cell Biol. 10, 251-337 (1994).
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 251-337
    • Van Der Geer, P.1    Hunter, T.2    Lindberg, R.A.3
  • 23
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: Implications for TNF receptor activation
    • Banner, D. W. et al. Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: implications for TNF receptor activation. Cell 73, 431-445 (1993).
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1
  • 24
    • 0026799307 scopus 로고
    • Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: Analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography
    • Sauter, N. K. et al. Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography. Biochemistry 31, 9609-9621 (1992).
    • (1992) Biochemistry , vol.31 , pp. 9609-9621
    • Sauter, N.K.1
  • 25
    • 0027196879 scopus 로고
    • Structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant 2.0 Å resolution
    • Delbaere, L. T. et al. Structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant 2.0 Å resolution. J. Mol. Biol. 230, 950-965 (1993).
    • (1993) J. Mol. Biol. , vol.230 , pp. 950-965
    • Delbaere, L.T.1
  • 26
    • 0003976860 scopus 로고
    • (eds Sawyer, L., Isaacs, N. & Bailey, S.) SERC Daresbury Laboratory, Warrington
    • Otwinowski, Z. & Minor, W. in Data Collection and Processing (eds Sawyer, L., Isaacs, N. & Bailey, S.) 556-562 (SERC Daresbury Laboratory, Warrington, 1993).
    • (1993) Data Collection and Processing , pp. 556-562
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for x-ray crystallography
    • CCP4. The CCP4 suite: programs for x-ray crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, 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    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 30
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.