메뉴 건너뛰기




Volumn 22, Issue 7, 2003, Pages 1555-1566

Structures of an ActRIIB:activin a complex reveal a novel binding mode for TGF-β ligand:receptor interactions

Author keywords

Activin; ActRIIB; Receptors; Signaling; Structure; TGF

Indexed keywords

ACTIVIN A; ACTIVIN RECEPTOR 2; ACTIVIN RECEPTOR 2B ACTIVIN A COMPLEX; DIMER; ISOPROTEIN; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 0345269804     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg156     Document Type: Article
Times cited : (181)

References (48)
  • 2
    • 0036333146 scopus 로고    scopus 로고
    • A changing morphogen gradient is interpreted by continuous transduction flow
    • Bourillot, P.Y., Garrett, N. and Gurdon, J.B. (2002) A changing morphogen gradient is interpreted by continuous transduction flow. Development, 129, 2167-2180.
    • (2002) Development , vol.129 , pp. 2167-2180
    • Bourillot, P.Y.1    Garrett, N.2    Gurdon, J.B.3
  • 3
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. (1998) Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D, 54, 905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 4
    • 0034733682 scopus 로고    scopus 로고
    • A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling
    • Chan, F.K., Chun, H.J., Zheng, L., Siegel, R.M., Bui, K.L. and Lenardo, M.J. (2000) A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling. Science, 288, 2351-2354.
    • (2000) Science , vol.288 , pp. 2351-2354
    • Chan, F.K.1    Chun, H.J.2    Zheng, L.3    Siegel, R.M.4    Bui, K.L.5    Lenardo, M.J.6
  • 5
    • 0037206410 scopus 로고    scopus 로고
    • Properties of inhibin binding to βglycan, InhBP/p120 and the activin type II receptors
    • Chapman, S.C., Bernard, D.J., Jelen, J. and Woodruff, T.K. (2002) Properties of inhibin binding to βglycan, InhBP/p120 and the activin type II receptors. Mol. Cell. Endocrinol., 196, 79.
    • (2002) Mol. Cell. Endocrinol. , vol.196 , pp. 79
    • Chapman, S.C.1    Bernard, D.J.2    Jelen, J.3    Woodruff, T.K.4
  • 6
    • 0028059199 scopus 로고
    • Homomeric interactions between type II transforming growth factor-β receptors
    • Chen, R.H. and Derynck, R. (1994) Homomeric interactions between type II transforming growth factor-β receptors. J. Biol. Chem., 269, 22868-22874.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22868-22874
    • Chen, R.H.1    Derynck, R.2
  • 7
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor-β2: An unusual fold for the superfamily
    • Daopin, S., Piez, K.A., Ogawa, Y. and Davies, D.R. (1992) Crystal structure of transforming growth factor-β2: an unusual fold for the superfamily. Science, 257, 369-373.
    • (1992) Science , vol.257 , pp. 369-373
    • Daopin, S.1    Piez, K.A.2    Ogawa, Y.3    Davies, D.R.4
  • 8
    • 0036587571 scopus 로고    scopus 로고
    • Transforming growth factor β signal transduction
    • Dennler, S., Goumans, M.J. and ten Dijke, P. (2002) Transforming growth factor β signal transduction. J. Leukoc. Biol., 71, 731-740.
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 731-740
    • Dennler, S.1    Goumans, M.J.2    Ten Dijke, P.3
  • 9
    • 0030989670 scopus 로고    scopus 로고
    • X-ray structure of glial cell-derived neurotrophic factor at 1.9 Å resolution and implications for receptor binding
    • Eigenbrot, C. and Gerber, N. (1997) X-ray structure of glial cell-derived neurotrophic factor at 1.9 Å resolution and implications for receptor binding. Nat. Struct. Biol., 4, 435-438.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 435-438
    • Eigenbrot, C.1    Gerber, N.2
  • 10
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella, T.W., Jr and Jovin, T.M. (1995) Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J. Cell Biol., 129, 1543-1558.
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella T.W., Jr.1    Jovin, T.M.2
  • 11
    • 0034021776 scopus 로고    scopus 로고
    • Bone morphogenetic protein receptor complexes on the surface of live cells: A new oligomerization mode for serine/threonine kinase receptors
    • Gilboa, L., Nohe, A., Geissendorfer, T., Sebald, W., Henis, Y.I. and Knaus, P. (2000) Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors. Mol. Biol. Cell, 11, 1023-1035.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1023-1035
    • Gilboa, L.1    Nohe, A.2    Geissendorfer, T.3    Sebald, W.4    Henis, Y.I.5    Knaus, P.6
  • 13
    • 0032899751 scopus 로고    scopus 로고
    • Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase
    • Greenwald, J., Fischer, W.H., Vale, W.W. and Choe, S. (1999) Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase. Nat. Struct. Biol., 6, 18-22.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 18-22
    • Greenwald, J.1    Fischer, W.H.2    Vale, W.W.3    Choe, S.4
  • 14
    • 0030042590 scopus 로고    scopus 로고
    • Three-dimensional structure of recombinant human osteogenic protein 1: Structural paradigm for the transforming growth factor β superfamily
    • Griffith, D.L., Keck, P.C., Sampath, T.K., Rueger, D.C. and Carlson, W.D. (1996) Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor β superfamily. Proc. Natl Acad. Sci. USA, 93, 878-883.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 878-883
    • Griffith, D.L.1    Keck, P.C.2    Sampath, T.K.3    Rueger, D.C.4    Carlson, W.D.5
  • 17
    • 0028291369 scopus 로고
    • The types II and III transforming growth factor-β receptors form homo-oligomers
    • Henis, Y.I., Moustakas, A., Lin, H.Y. and Lodish, H.F. (1994) The types II and III transforming growth factor-β receptors form homo-oligomers. J. Cell Biol., 126, 139-154.
    • (1994) J. Cell Biol. , vol.126 , pp. 139-154
    • Henis, Y.I.1    Moustakas, A.2    Lin, H.Y.3    Lodish, H.F.4
  • 18
    • 8944220232 scopus 로고    scopus 로고
    • Transforming growth factor β1: Three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor β2
    • Hinck, A.P. et al. (1996) Transforming growth factor β1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor β2. Biochemistry, 35, 8517-8534.
    • (1996) Biochemistry , vol.35 , pp. 8517-8534
    • Hinck, A.P.1
  • 19
    • 0034459679 scopus 로고    scopus 로고
    • Evolutionary trace analysis of TGF-β and related growth factors: Implications for site-directed mutagenesis
    • Innis, C.A., Shi, J. and Blundell, T.L. (2000) Evolutionary trace analysis of TGF-β and related growth factors: implications for site-directed mutagenesis. Protein Eng., 13, 839-847.
    • (2000) Protein Eng. , vol.13 , pp. 839-847
    • Innis, C.A.1    Shi, J.2    Blundell, T.L.3
  • 20
    • 0034600953 scopus 로고    scopus 로고
    • BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II
    • Kirsch, T., Nickel, J. and Sebald, W. (2000a) BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II. EMBO J., 19, 3314-3324.
    • (2000) EMBO J. , vol.19 , pp. 3314-3324
    • Kirsch, T.1    Nickel, J.2    Sebald, W.3
  • 21
    • 0034043106 scopus 로고    scopus 로고
    • Crystal structure of the BMP-2-BRIA ectodomain complex
    • Kirsch, T., Sebald, W. and Dreyer, M.K. (2000b) Crystal structure of the BMP-2-BRIA ectodomain complex. Nat. Struct. Biol., 7, 492-496.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 492-496
    • Kirsch, T.1    Sebald, W.2    Dreyer, M.K.3
  • 22
    • 0033624022 scopus 로고    scopus 로고
    • Activin βC and βE genes are not essential for mouse liver growth, differentiation, and regeneration
    • Lau, A.L., Kumar, T.R., Nishimori, K., Bonadio, J. and Matzuk, M.M. (2000) Activin βC and βE genes are not essential for mouse liver growth, differentiation, and regeneration. Mol. Cell. Biol., 20, 6127-6137.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6127-6137
    • Lau, A.L.1    Kumar, T.R.2    Nishimori, K.3    Bonadio, J.4    Matzuk, M.M.5
  • 23
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah, O., Stura, E.A., Middleton, S.A., Johnson, D.L., Jolliffe, L.K. and Wilson, I.A. (1999) Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science, 283, 987-990.
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1    Stura, E.A.2    Middleton, S.A.3    Johnson, D.L.4    Jolliffe, L.K.5    Wilson, I.A.6
  • 24
    • 0030972496 scopus 로고    scopus 로고
    • Positive and negative regulation of type II TGF-β receptor signal transduction by autophosphorylation on multiple serine residues
    • Luo, K. and Lodish, H.F. (1997) Positive and negative regulation of type II TGF-β receptor signal transduction by autophosphorylation on multiple serine residues. EMBO J., 16, 1970-1981.
    • (1997) EMBO J. , vol.16 , pp. 1970-1981
    • Luo, K.1    Lodish, H.F.2
  • 25
    • 0034574298 scopus 로고    scopus 로고
    • How cells read TGF-β signals
    • Massagué, J. (2000) How cells read TGF-β signals. Nat. Rev. Mol. Cell Biol., 1, 169-178.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 169-178
    • Massagué, J.1
  • 26
    • 0034654497 scopus 로고    scopus 로고
    • Controlling TGF-β signaling
    • Massagué, J. and Chen, Y.G. (2000) Controlling TGF-β signaling. Genes Dev., 14, 627-644.
    • (2000) Genes Dev. , vol.14 , pp. 627-644
    • Massagué, J.1    Chen, Y.G.2
  • 27
    • 0029904671 scopus 로고    scopus 로고
    • Serine/threonine kinase receptors: Mediators of transforming growth factor β family signals
    • Massagué, J. and Weis-Garcia, F. (1996) Serine/threonine kinase receptors: mediators of transforming growth factor β family signals. Cancer Surv., 27, 41-64.
    • (1996) Cancer Surv. , vol.27 , pp. 41-64
    • Massagué, J.1    Weis-Garcia, F.2
  • 28
    • 0034678908 scopus 로고    scopus 로고
    • Transcriptional control by the TGF-β/Smad signaling system
    • Massagué, J. and Wotton, D. (2000) Transcriptional control by the TGF-β/Smad signaling system. EMBO J., 19, 1745-1754.
    • (2000) EMBO J. , vol.19 , pp. 1745-1754
    • Massagué, J.1    Wotton, D.2
  • 29
    • 0034644472 scopus 로고    scopus 로고
    • TGFβ signaling in growth control, cancer, and heritable disorders
    • Massagué, J., Blain, S.W. and Lo, R.S. (2000) TGFβ signaling in growth control, cancer, and heritable disorders. Cell, 103, 295-309.
    • (2000) Cell , vol.103 , pp. 295-309
    • Massagué, J.1    Blain, S.W.2    Lo, R.S.3
  • 31
    • 0029943464 scopus 로고    scopus 로고
    • The crystal structure of TGF-β3 and comparison to TGF-β2: Implications for receptor binding
    • Mittl, P.R., Priestle, J.P., Cox, D.A., McMaster, G., Cerletti, N. and Grutter, M.G. (1996) The crystal structure of TGF-β3 and comparison to TGF-β2: implications for receptor binding. Protein Sci., 5, 1261-1271.
    • (1996) Protein Sci. , vol.5 , pp. 1261-1271
    • Mittl, P.R.1    Priestle, J.P.2    Cox, D.A.3    McMaster, G.4    Cerletti, N.5    Grutter, M.G.6
  • 32
    • 0035032914 scopus 로고    scopus 로고
    • Divergence and convergence of TGF-β/BMP signaling
    • Miyazono, K., Kusanagi, K. and Inoue, H. (2001) Divergence and convergence of TGF-β/BMP signaling. J. Cell Physiol., 187, 265-276.
    • (2001) J. Cell Physiol. , vol.187 , pp. 265-276
    • Miyazono, K.1    Kusanagi, K.2    Inoue, H.3
  • 33
    • 0037085287 scopus 로고    scopus 로고
    • The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways
    • Nohe, A., Hassel, S., Ehrlich, M., Neubauer, F., Sebald, W., Henis, Y.I. and Knaus, P. (2002) The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways. J. Biol. Chem., 277, 5330-5338.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5330-5338
    • Nohe, A.1    Hassel, S.2    Ehrlich, M.3    Neubauer, F.4    Sebald, W.5    Henis, Y.I.6    Knaus, P.7
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0036148596 scopus 로고    scopus 로고
    • Production and purification of recombinant human inhibin and activin
    • Pangas, S.A. and Woodruff, T.K. (2002) Production and purification of recombinant human inhibin and activin. J. Endocrinol., 172, 199-210.
    • (2002) J. Endocrinol. , vol.172 , pp. 199-210
    • Pangas, S.A.1    Woodruff, T.K.2
  • 36
    • 0035153463 scopus 로고    scopus 로고
    • Role of transforming growth factor β in cancer
    • Pasche, B. (2001) Role of transforming growth factor β in cancer. J. Cell. Physiol., 186, 153-168.
    • (2001) J. Cell. Physiol. , vol.186 , pp. 153-168
    • Pasche, B.1
  • 37
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R.J. (2001) Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D, 57, 1373-1382.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 38
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy, I., Wilson, I.A. and Michnick, S.W. (1999) Erythropoietin receptor activation by a ligand-induced conformation change. Science, 283, 990-993.
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 39
    • 0034214305 scopus 로고    scopus 로고
    • The Xenopus eomesodermin promoter and its concentration-dependent response to activin
    • Ryan, K., Garrett, N., Bourillot, P., Stennard, F. and Gurdon, J.B. (2000) The Xenopus eomesodermin promoter and its concentration-dependent response to activin. Mech. Dev., 94, 133-146.
    • (2000) Mech. Dev. , vol.94 , pp. 133-146
    • Ryan, K.1    Garrett, N.2    Bourillot, P.3    Stennard, F.4    Gurdon, J.B.5
  • 40
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako, Y., Minoghchi, S. and Yanagida, T. (2000) Single-molecule imaging of EGFR signalling on the surface of living cells. Nat. Cell Biol., 2, 168-172.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 41
    • 0033582942 scopus 로고    scopus 로고
    • Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution
    • Scheufler, C., Sebald, W. and Hulsmeyer, M. (1999) Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution. J. Mol. Biol., 287, 103-115.
    • (1999) J. Mol. Biol. , vol.287 , pp. 103-115
    • Scheufler, C.1    Sebald, W.2    Hulsmeyer, M.3
  • 42
    • 0026633842 scopus 로고
    • An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth factor-β2
    • Schlunegger, M.P. and Grutter, M.G. (1992) An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth factor-β2. Nature, 358, 430-434.
    • (1992) Nature , vol.358 , pp. 430-434
    • Schlunegger, M.P.1    Grutter, M.G.2
  • 43
    • 0032188942 scopus 로고    scopus 로고
    • Efficiency of signalling through cytokine receptors depends critically on receptor orientation
    • Syed, R.S. et al. (1998) Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature, 395, 511-516.
    • (1998) Nature , vol.395 , pp. 511-516
    • Syed, R.S.1
  • 44
    • 0036232693 scopus 로고    scopus 로고
    • Expression and dimerization of the rat activin subunits βC and βE: Evidence for the formation of novel activin dimers
    • Vejda, S., Cranfield, M., Peter, B., Mellor, S.L., Groome, N., Schulte-Hermann, R. and Rossmanith, W. (2002) Expression and dimerization of the rat activin subunits βC and βE: evidence for the formation of novel activin dimers. J. Mol. Endocrinol., 28, 137-148.
    • (2002) J. Mol. Endocrinol. , vol.28 , pp. 137-148
    • Vejda, S.1    Cranfield, M.2    Peter, B.3    Mellor, S.L.4    Groome, N.5    Schulte-Hermann, R.6    Rossmanith, W.7
  • 45
    • 0033605117 scopus 로고    scopus 로고
    • Transforming growth factor-β induces formation of a dithiothreitol-resistant Type I/Type II receptor complex in live cells
    • Wells, R.G., Gilboa, L., Sun, Y., Liu, X., Henis, Y.I. and Lodish, H.F. (1999) Transforming growth factor-β induces formation of a dithiothreitol-resistant Type I/Type II receptor complex in live cells. J. Biol. Chem., 274, 5716-5722.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5716-5722
    • Wells, R.G.1    Gilboa, L.2    Sun, Y.3    Liu, X.4    Henis, Y.I.5    Lodish, H.F.6
  • 46
    • 0032055268 scopus 로고    scopus 로고
    • Regulation of cellular and system function by activin
    • Woodruff, T.K. (1998) Regulation of cellular and system function by activin. Biochem. Pharmacol., 55, 953-963.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 953-963
    • Woodruff, T.K.1
  • 47
    • 0028942852 scopus 로고
    • Inhibin, activin and the female reproductive axis
    • Woodruff, T.K. and Mather, J.P. (1995) Inhibin, activin and the female reproductive axis. Annu. Rev. Physiol., 57, 219-244.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 219-244
    • Woodruff, T.K.1    Mather, J.P.2
  • 48
    • 0033515443 scopus 로고    scopus 로고
    • Identification of two amino acids in activin A that are important for biological activity and binding to the activin type II receptors
    • Wuytens, G. et al. (1999) Identification of two amino acids in activin A that are important for biological activity and binding to the activin type II receptors. J. Biol. Chem., 274, 9821-9827.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9821-9827
    • Wuytens, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.