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Volumn 25, Issue 2, 2017, Pages 341-352

Structure of the Full-length VEGFR-1 Extracellular Domain in Complex with VEGF-A

Author keywords

angiogenesis; extracellular domain; receptor tyrosine kinase; single particle negative stain electron microscopy; small angle X ray scattering; vascular endothelial growth factor; VEGF receptor; X ray crystallography

Indexed keywords

IMMUNOGLOBULIN; VASCULOTROPIN A; VASCULOTROPIN RECEPTOR 1; VASCULOTROPIN RECEPTOR 2; LIGAND; PROTEIN BINDING; RECOMBINANT PROTEIN; VEGFA PROTEIN, HUMAN;

EID: 85009799929     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2016.12.012     Document Type: Article
Times cited : (75)

References (58)
  • 4
    • 79960690759 scopus 로고    scopus 로고
    • Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output
    • Ballmer-Hofer, K., Andersson, A.E., Ratcliffe, L.E., Berger, P., Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output. Blood 118 (2011), 816–826.
    • (2011) Blood , vol.118 , pp. 816-826
    • Ballmer-Hofer, K.1    Andersson, A.E.2    Ratcliffe, L.E.3    Berger, P.4
  • 5
    • 0030932842 scopus 로고    scopus 로고
    • Mapping of the sites for ligand binding and receptor dimerization at the extracellular domain of the vascular endothelial growth factor receptor FLT-1
    • Barleon, B., Totzke, F., Herzog, C., Blanke, S., Kremmer, E., Siemeister, G., Marmé, D., Martiny-Baron, G., Mapping of the sites for ligand binding and receptor dimerization at the extracellular domain of the vascular endothelial growth factor receptor FLT-1. J. Biol. Chem. 272 (1997), 10382–10388.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10382-10388
    • Barleon, B.1    Totzke, F.2    Herzog, C.3    Blanke, S.4    Kremmer, E.5    Siemeister, G.6    Marmé, D.7    Martiny-Baron, G.8
  • 9
    • 1642297115 scopus 로고    scopus 로고
    • The crystal structure of PlGF in complex with domain 2 of VEGFR1
    • Christinger, H.W., Fuh, G., de Vos, A.M., Wiesmann, C., The crystal structure of PlGF in complex with domain 2 of VEGFR1. J. Biol. Chem. 279 (2004), 10382–10388.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10382-10388
    • Christinger, H.W.1    Fuh, G.2    de Vos, A.M.3    Wiesmann, C.4
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. Biol. Crystallogr. 50 (1994), 760–763.
    • (1994) Acta Crystallogr. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 12
    • 0345989988 scopus 로고    scopus 로고
    • Crystallography of biological macromolecules
    • E. Arnold D.M. Himmel M.G. Rossmann International Union of Crystallography
    • Cowtan, K., Zhang, K., Main, P., Crystallography of biological macromolecules. Arnold, E., Himmel, D.M., Rossmann, M.G., (eds.) International Tables for Crystallography Volume F, 2012, International Union of Crystallography, 385–400.
    • (2012) International Tables for Crystallography Volume F , pp. 385-400
    • Cowtan, K.1    Zhang, K.2    Main, P.3
  • 15
    • 0029790466 scopus 로고    scopus 로고
    • The second immunoglobulin-like domain of the VEGF tyrosine kinase receptor Flt-1 determines ligand binding and may initiate a signal transduction cascade
    • Davis-Smyth, T., Chen, H., Park, J., Presta, L.G., Ferrara, N., The second immunoglobulin-like domain of the VEGF tyrosine kinase receptor Flt-1 determines ligand binding and may initiate a signal transduction cascade. EMBO J. 15 (1996), 4919–4927.
    • (1996) EMBO J. , vol.15 , pp. 4919-4927
    • Davis-Smyth, T.1    Chen, H.2    Park, J.3    Presta, L.G.4    Ferrara, N.5
  • 16
    • 75149176738 scopus 로고    scopus 로고
    • Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers
    • Dell'Era Dosch, D., Ballmer-Hofer, K., Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers. FASEB J. 24 (2010), 32–38.
    • (2010) FASEB J. , vol.24 , pp. 32-38
    • Dell'Era Dosch, D.1    Ballmer-Hofer, K.2
  • 18
    • 0029021660 scopus 로고
    • Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium
    • Fong, G.H., Rossant, J., Gertsenstein, M., Breitman, M.L., Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium. Nature 376 (1995), 66–70.
    • (1995) Nature , vol.376 , pp. 66-70
    • Fong, G.H.1    Rossant, J.2    Gertsenstein, M.3    Breitman, M.L.4
  • 20
    • 0032482978 scopus 로고    scopus 로고
    • Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice
    • Hiratsuka, S., Minowa, O., Kuno, J., Noda, T., Shibuya, M., Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice. Proc. Natl. Acad. Sci. USA 95 (1998), 9349–9354.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9349-9354
    • Hiratsuka, S.1    Minowa, O.2    Kuno, J.3    Noda, T.4    Shibuya, M.5
  • 21
    • 0035114105 scopus 로고    scopus 로고
    • Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor receptor-1) in pathological angiogenesis
    • Hiratsuka, S., Maru, Y., Okada, A., Seiki, M., Noda, T., Shibuya, M., Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor receptor-1) in pathological angiogenesis. Cancer Res. 61 (2001), 1207–1213.
    • (2001) Cancer Res. , vol.61 , pp. 1207-1213
    • Hiratsuka, S.1    Maru, Y.2    Okada, A.3    Seiki, M.4    Noda, T.5    Shibuya, M.6
  • 24
    • 77954912465 scopus 로고    scopus 로고
    • Structural insights into the binding of VEGF-B by VEGFR-1D2: recognition and specificity
    • Iyer, S., Darley, P.I., Acharya, K.R., Structural insights into the binding of VEGF-B by VEGFR-1D2: recognition and specificity. J. Biol. Chem. 285 (2010), 23779–23789.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23779-23789
    • Iyer, S.1    Darley, P.I.2    Acharya, K.R.3
  • 25
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W., Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993), 795–800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 26
    • 0027421333 scopus 로고
    • Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor
    • Kendall, R.L., Thomas, K.A., Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor. Proc. Natl. Acad. Sci. USA 90 (1993), 10705–10709.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10705-10709
    • Kendall, R.L.1    Thomas, K.A.2
  • 28
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon, M.A., Schlessinger, J., Cell signaling by receptor tyrosine kinases. Cell 141 (2010), 1117–1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 32
    • 0037370337 scopus 로고    scopus 로고
    • Soluble VEGF receptor Flt1: the elusive preeclampsia factor discovered?
    • Luttun, A., Carmeliet, P., Soluble VEGF receptor Flt1: the elusive preeclampsia factor discovered?. J. Clin. Invest. 111 (2003), 600–602.
    • (2003) J. Clin. Invest. , vol.111 , pp. 600-602
    • Luttun, A.1    Carmeliet, P.2
  • 35
    • 0037373006 scopus 로고    scopus 로고
    • Excess placental soluble fms-like tyrosine kinase 1 (sFlt1) may contribute to endothelial dysfunction, hypertension, and proteinuria in preeclampsia
    • Maynard, S.E., Min, J.Y., Merchan, J., Lim, K.H., Li, J., Mondal, S., Libermann, T.A., Morgan, J.P., Sellke, F.W., Stillman, I.E., et al. Excess placental soluble fms-like tyrosine kinase 1 (sFlt1) may contribute to endothelial dysfunction, hypertension, and proteinuria in preeclampsia. J. Clin. Invest. 111 (2003), 649–658.
    • (2003) J. Clin. Invest. , vol.111 , pp. 649-658
    • Maynard, S.E.1    Min, J.Y.2    Merchan, J.3    Lim, K.H.4    Li, J.5    Mondal, S.6    Libermann, T.A.7    Morgan, J.P.8    Sellke, F.W.9    Stillman, I.E.10
  • 37
    • 52949142769 scopus 로고    scopus 로고
    • Functional and structural stability of the epidermal growth factor receptor in detergent micelles and phospholipid nanodiscs
    • Mi, L.Z., Grey, M.J., Nishida, N., Walz, T., Lu, C., Springer, T.A., Functional and structural stability of the epidermal growth factor receptor in detergent micelles and phospholipid nanodiscs. Biochemistry 47 (2008), 10314–10323.
    • (2008) Biochemistry , vol.47 , pp. 10314-10323
    • Mi, L.Z.1    Grey, M.J.2    Nishida, N.3    Walz, T.4    Lu, C.5    Springer, T.A.6
  • 38
  • 39
    • 84893474573 scopus 로고    scopus 로고
    • Structure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers
    • Opatowsky, Y., Lax, I., Tome, F., Bleichert, F., Unger, V.M., Schlessinger, J., Structure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers. Proc. Natl. Acad. Sci. USA 111 (2014), 1772–1777.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 1772-1777
    • Opatowsky, Y.1    Lax, I.2    Tome, F.3    Bleichert, F.4    Unger, V.M.5    Schlessinger, J.6
  • 40
    • 84920559004 scopus 로고    scopus 로고
    • The strength and cooperativity of KIT ectodomain contacts determine normal ligand-dependent stimulation or oncogenic activation in cancer
    • Reshetnyak, A.V., Opatowsky, Y., Boggon, T.J., Folta-Stogniew, E., Tome, F., Lax, I., Schlessinger, J., The strength and cooperativity of KIT ectodomain contacts determine normal ligand-dependent stimulation or oncogenic activation in cancer. Mol. Cell 57 (2015), 191–201.
    • (2015) Mol. Cell , vol.57 , pp. 191-201
    • Reshetnyak, A.V.1    Opatowsky, Y.2    Boggon, T.J.3    Folta-Stogniew, E.4    Tome, F.5    Lax, I.6    Schlessinger, J.7
  • 42
    • 36349030423 scopus 로고    scopus 로고
    • Placental growth factor-1 attenuates vascular endothelial growth factor-A-dependent tumor angiogenesis during beta cell carcinogenesis
    • Schomber, T., Kopfstein, L., Djonov, V., Albrecht, I., Baeriswyl, V., Strittmatter, K., Christofori, G., Placental growth factor-1 attenuates vascular endothelial growth factor-A-dependent tumor angiogenesis during beta cell carcinogenesis. Cancer Res. 67 (2007), 10840–10848.
    • (2007) Cancer Res. , vol.67 , pp. 10840-10848
    • Schomber, T.1    Kopfstein, L.2    Djonov, V.3    Albrecht, I.4    Baeriswyl, V.5    Strittmatter, K.6    Christofori, G.7
  • 44
    • 84885028426 scopus 로고    scopus 로고
    • VEGFR and type-V RTK activation and signaling
    • Shibuya, M., VEGFR and type-V RTK activation and signaling. Cold Spring Harb. Perspect. Biol., 5, 2013, a009092.
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5 , pp. a009092
    • Shibuya, M.1
  • 45
    • 84893148365 scopus 로고    scopus 로고
    • VEGF-VEGFR signals in health and disease
    • Shibuya, M., VEGF-VEGFR signals in health and disease. Biomol. Ther. 22 (2014), 1–9.
    • (2014) Biomol. Ther. , vol.22 , pp. 1-9
    • Shibuya, M.1
  • 46
    • 0032553425 scopus 로고    scopus 로고
    • Mapping of the sites involved in ligand association and dissociation at the extracellular domain of the kinase insert domain-containing receptor for vascular endothelial growth factor
    • Shinkai, A., Ito, M., Anazawa, H., Yamaguchi, S., Shitara, K., Shibuya, M., Mapping of the sites involved in ligand association and dissociation at the extracellular domain of the kinase insert domain-containing receptor for vascular endothelial growth factor. J. Biol. Chem. 273 (1998), 31283–31288.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31283-31288
    • Shinkai, A.1    Ito, M.2    Anazawa, H.3    Yamaguchi, S.4    Shitara, K.5    Shibuya, M.6
  • 48
    • 48149098354 scopus 로고    scopus 로고
    • DARPins: a new generation of protein therapeutics
    • Stumpp, M.T., Binz, H.K., Amstutz, P., DARPins: a new generation of protein therapeutics. Drug Discov. Today 13 (2008), 695–701.
    • (2008) Drug Discov. Today , vol.13 , pp. 695-701
    • Stumpp, M.T.1    Binz, H.K.2    Amstutz, P.3
  • 54
    • 0030782410 scopus 로고    scopus 로고
    • Crystal structure at 1.7 Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor
    • Wiesmann, C., Fuh, G., Christinger, H.W., Eigenbrot, C., Wells, J.A., de Vos, A.M., Crystal structure at 1.7 Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Cell 91 (1997), 695–704.
    • (1997) Cell , vol.91 , pp. 695-704
    • Wiesmann, C.1    Fuh, G.2    Christinger, H.W.3    Eigenbrot, C.4    Wells, J.A.5    de Vos, A.M.6
  • 55
    • 45549109855 scopus 로고    scopus 로고
    • Contacts between membrane proximal regions of the PDGF receptor ectodomain are required for receptor activation but not for receptor dimerization
    • Yang, Y., Yuzawa, S., Schlessinger, J., Contacts between membrane proximal regions of the PDGF receptor ectodomain are required for receptor activation but not for receptor dimerization. Proc. Natl. Acad. Sci. USA 105 (2008), 7681–7686.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7681-7686
    • Yang, Y.1    Yuzawa, S.2    Schlessinger, J.3
  • 56
    • 76649105135 scopus 로고    scopus 로고
    • Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling
    • Yang, Y., Xie, P., Opatowsky, Y., Schlessinger, J., Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling. Proc. Natl. Acad. Sci. USA 107 (2010), 1906–1911.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1906-1911
    • Yang, Y.1    Xie, P.2    Opatowsky, Y.3    Schlessinger, J.4
  • 57
    • 34447531743 scopus 로고    scopus 로고
    • Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor
    • Yuzawa, S., Opatowsky, Y., Zhang, Z., Mandiyan, V., Lax, I., Schlessinger, J., Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor. Cell 130 (2007), 323–334.
    • (2007) Cell , vol.130 , pp. 323-334
    • Yuzawa, S.1    Opatowsky, Y.2    Zhang, Z.3    Mandiyan, V.4    Lax, I.5    Schlessinger, J.6
  • 58
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y., I-TASSER server for protein 3D structure prediction. BMC Bioinformatics, 9, 2008, 40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1


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