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Volumn 16, Issue 16, 1997, Pages 4999-5005

NMR structure of the death domain of the p75 neurotrophin receptor

Author keywords

Death domain; NMR; p75 neurotrophin receptor

Indexed keywords

FAS ANTIGEN; NEUROTROPHIN RECEPTOR; SERINE; THREONINE; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 0030851905     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.16.4999     Document Type: Article
Times cited : (265)

References (50)
  • 2
    • 0027966170 scopus 로고
    • Disruption of NGF binding to the low affinity neurotrophin receptor p75(LNTR) reduces NGF binding to TrkA on PC12 cells
    • Barker, P.A. and Shooter, E.M. (1994) Disruption of NGF binding to the low affinity neurotrophin receptor p75(LNTR) reduces NGF binding to TrkA on PC12 cells. Neuron, 13, 203-215.
    • (1994) Neuron , vol.13 , pp. 203-215
    • Barker, P.A.1    Shooter, E.M.2
  • 3
    • 0028270620 scopus 로고
    • The p75 nerve growth factor receptor mediates survival or death depending on the stage of sensory neuron development
    • Barrett, G.L. and Bartlett, P.F. (1994) The p75 nerve growth factor receptor mediates survival or death depending on the stage of sensory neuron development. Proc. Natl Acad. Sci. USA, 91, 6501-6505.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6501-6505
    • Barrett, G.L.1    Bartlett, P.F.2
  • 5
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin, M.P., Varfolomeev, E.E., Pancer, Z., Mett, I.L., Camonis, J.H. and Wallach, D. (1995) A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J. Biol. Chem., 270, 7795-7798.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 6
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin, M.P., Goncharov, T.M., Goltsev, Y.V. and Wallach, D. (1996) Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1-and TNF receptor-induced cell death. Cell, 85, 803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 9
    • 0029805770 scopus 로고    scopus 로고
    • Death of oligodendrocytes mediated by the interaction of nerve growth factor with its receptor p75
    • Casaccia-Bonnefil, P., Carter, B.D., Dobrowsky, R.T. and Chao, M.V. (1996) Death of oligodendrocytes mediated by the interaction of nerve growth factor with its receptor p75. Nature, 383,
    • (1996) Nature , vol.383
    • Casaccia-Bonnefil, P.1    Carter, B.D.2    Dobrowsky, R.T.3    Chao, M.V.4
  • 12
    • 0028843735 scopus 로고
    • A region of the 75 kDa neurotrophin receptor homologous to the death domains of TNFR-I and Fas
    • Chapman, B.S. (1995) A region of the 75 kDa neurotrophin receptor homologous to the death domains of TNFR-I and Fas. FEBS Lett., 374, 216-220.
    • (1995) FEBS Lett. , vol.374 , pp. 216-220
    • Chapman, B.S.1
  • 13
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan, A.M., O'Rourke, K., Tewari, M. and Dixit, V.M. (1995) FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell, 81, 505-512.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 14
    • 0028108788 scopus 로고
    • Activation of the sphingomyelin cycle through the low-affinity neurotrophin receptor
    • Dobrowsky, R., Werner, M., Castellino, A., Chao, M. and Hannun, Y. (1994) Activation of the sphingomyelin cycle through the low-affinity neurotrophin receptor. Science, 265, 1596-1599.
    • (1994) Science , vol.265 , pp. 1596-1599
    • Dobrowsky, R.1    Werner, M.2    Castellino, A.3    Chao, M.4    Hannun, Y.5
  • 15
    • 0029090337 scopus 로고
    • Neurotrophins induce sphingomyelin hydrolysis - Modulation by co-expression of p75(NTR) with trk receptors
    • Dobrowsky, R.T., Jenkins, G.M. and Hannun, Y.A. (1995) Neurotrophins induce sphingomyelin hydrolysis - modulation by co-expression of p75(NTR) with trk receptors. J. Biol. Chem., 270, 22135-22142.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22135-22142
    • Dobrowsky, R.T.1    Jenkins, G.M.2    Hannun, Y.A.3
  • 16
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • Duan, H. and Dixit, V.M. (1997) RAIDD is a new 'death' adaptor molecule. Nature, 385, 86-89.
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 18
  • 19
    • 0029787071 scopus 로고    scopus 로고
    • Induction of cell death by endogenous nerve growth factor through its p75 receptor
    • Frade, J.M., Rodriguez-Tébar, A. and Barde, Y.A. (1996) Induction of cell death by endogenous nerve growth factor through its p75 receptor. Nature, 383, 166-168.
    • (1996) Nature , vol.383 , pp. 166-168
    • Frade, J.M.1    Rodriguez-Tébar, A.2    Barde, Y.A.3
  • 20
    • 0029649665 scopus 로고
    • Homology between reaper and the cell death domains of Fas and TNFR1
    • Golstein, P., Marguet, D. and Depraetere, V. (1995) Homology between reaper and the cell death domains of Fas and TNFR1. Cell, 81, 185-186.
    • (1995) Cell , vol.81 , pp. 185-186
    • Golstein, P.1    Marguet, D.2    Depraetere, V.3
  • 21
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert, P., Braun, W. and Wüthrich, K. (1991) Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217, 517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 22
    • 0027939697 scopus 로고
    • The low-affinity NGF receptor can collaborate with each of the Trks to potentiate functional responses to the neurotrophins
    • Hantzopoulos, P., Suri, C., Glass, D., Goldfab, M. and Yancopoulos, G. (1994) The low-affinity NGF receptor can collaborate with each of the Trks to potentiate functional responses to the neurotrophins. Neuron, 13, 187-201.
    • (1994) Neuron , vol.13 , pp. 187-201
    • Hantzopoulos, P.1    Suri, C.2    Glass, D.3    Goldfab, M.4    Yancopoulos, G.5
  • 23
    • 0025774207 scopus 로고
    • High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor
    • Hempstead, B., Martin-Zanca, D., Kaplan, D., Parada, L. and Chao, M. (1991) High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor. Nature, 350, 678-683.
    • (1991) Nature , vol.350 , pp. 678-683
    • Hempstead, B.1    Martin-Zanca, D.2    Kaplan, D.3    Parada, L.4    Chao, M.5
  • 24
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 25
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation
    • Hsu, H.L., Xiong, J. and Goeddel, D.V. (1995) The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell, 81, 495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.L.1    Xiong, J.2    Goeddel, D.V.3
  • 26
    • 0030465072 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the Fas (Apo-1/CD95) death domain
    • Huang, B.H., Eberstadt, M., Olejniczak, E.T., Meadows, R.P. and Fesik, S.W. (1996) NMR structure and mutagenesis of the Fas (Apo-1/CD95) death domain. Nature, 384, 638-641.
    • (1996) Nature , vol.384 , pp. 638-641
    • Huang, B.H.1    Eberstadt, M.2    Olejniczak, E.T.3    Meadows, R.P.4    Fesik, S.W.5
  • 28
    • 0025735392 scopus 로고
    • The trk proto-oncogene product: A signal transducing receptor for nerve growth factor
    • Kaplan, D., Hempstead, B., Martin-Zanca, D., Chao, M. and Parada, L. (1991) The trk proto-oncogene product: a signal transducing receptor for nerve growth factor. Science, 252, 554-558.
    • (1991) Science , vol.252 , pp. 554-558
    • Kaplan, D.1    Hempstead, B.2    Martin-Zanca, D.3    Chao, M.4    Parada, L.5
  • 29
    • 0025857391 scopus 로고
    • The trk proto-oncogene encodes a receptor for nerve growth factor
    • Klein, R., Jing, S., Nanduri, V., O'Rourke, E. and Barbacid, M. (1991) The trk proto-oncogene encodes a receptor for nerve growth factor. Cell, 65, 189-197.
    • (1991) Cell , vol.65 , pp. 189-197
    • Klein, R.1    Jing, S.2    Nanduri, V.3    O'Rourke, E.4    Barbacid, M.5
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 31
    • 0029892470 scopus 로고    scopus 로고
    • Physiology of neurotrophins
    • Lewin, G. and Barde, Y.-A. (1996) Physiology of neurotrophins. Annu. Rev. Neurosci., 19, 289-317.
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 289-317
    • Lewin, G.1    Barde, Y.-A.2
  • 32
    • 0028242139 scopus 로고
    • Solution structure and dynamics of PEC-60, a protein of the Kazal-type inhibitor family, determined by nuclear magnetic resonance
    • Liepinsh, E., Berndt, K.D., Sillard, R., Mutt, V. and Otting, G. (1994) Solution structure and dynamics of PEC-60, a protein of the Kazal-type inhibitor family, determined by nuclear magnetic resonance. J. Mol. Biol., 239, 137-153.
    • (1994) J. Mol. Biol. , vol.239 , pp. 137-153
    • Liepinsh, E.1    Berndt, K.D.2    Sillard, R.3    Mutt, V.4    Otting, G.5
  • 33
    • 0030236215 scopus 로고    scopus 로고
    • The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules
    • Luginbühl, P., Güntert, P., Billeter, M. and Wüthrich, K. (1996) The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules. J. Biomol. NMR, 8, 136-146.
    • (1996) J. Biomol. NMR , vol.8 , pp. 136-146
    • Luginbühl, P.1    Güntert, P.2    Billeter, M.3    Wüthrich, K.4
  • 34
    • 0028217645 scopus 로고
    • High affinity nerve growth factor binding displays a faster rate of association than p140(Trk) binding - Implications for multi-subunit polypeptide receptors
    • Mahadeo, D., Kaplan, L., Chao, M.V. and Hempstead, B.L. (1994) High affinity nerve growth factor binding displays a faster rate of association than p140(Trk) binding - implications for multi-subunit polypeptide receptors. J. Biol. Chem., 269, 6884-6891.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6884-6891
    • Mahadeo, D.1    Kaplan, L.2    Chao, M.V.3    Hempstead, B.L.4
  • 35
    • 0000372198 scopus 로고
    • The use of osmolytes to facilitate protein NMR spectroscopy
    • Matthews, S.J. and Leatherbarrow, R.J. (1993) The use of osmolytes to facilitate protein NMR spectroscopy. J. Biomol. NMR, 3, 597-600.
    • (1993) J. Biomol. NMR , vol.3 , pp. 597-600
    • Matthews, S.J.1    Leatherbarrow, R.J.2
  • 36
    • 0026766860 scopus 로고
    • The nerve growth factor family of receptors
    • Meakin, S.O. and Shooter, E.M. (1992) The nerve growth factor family of receptors. Trends Neurosci., 15, 323-331.
    • (1992) Trends Neurosci. , vol.15 , pp. 323-331
    • Meakin, S.O.1    Shooter, E.M.2
  • 37
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio, M. et al. (1996) FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell, 85, 817-827.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1
  • 38
    • 0029967670 scopus 로고    scopus 로고
    • Systematic mutational analysis of the death domain of the tumor necrosis factor receptor 1-associated protein TRADD
    • Park, A. and Baichwal, V.R. (1996) Systematic mutational analysis of the death domain of the tumor necrosis factor receptor 1-associated protein TRADD. J. Biol. Chem., 271, 9858-9862.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9858-9862
    • Park, A.1    Baichwal, V.R.2
  • 40
    • 0023133256 scopus 로고
    • Gene transfer and molecular cloning of the rat nerve growth factor receptor
    • Radeke, M.J., Misko, T.P., Hsu, C., Herzenberg, L.A. and Shooter, E.M. (1987) Gene transfer and molecular cloning of the rat nerve growth factor receptor. Nature, 325, 593-597.
    • (1987) Nature , vol.325 , pp. 593-597
    • Radeke, M.J.1    Misko, T.P.2    Hsu, C.3    Herzenberg, L.A.4    Shooter, E.M.5
  • 41
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson, J.S. and Richardson, D.C. (1988) Amino acid preferences for specific locations at the ends of alpha helices. Science, 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 42
    • 0025321521 scopus 로고
    • Binding of brain-derived neurotrophic factor to the nerve growth factor receptor
    • Rodriguez-Tébar, A., Dechant, G. and Barde, Y.-A. (1990) Binding of brain-derived neurotrophic factor to the nerve growth factor receptor. Neuron, 4, 487-492.
    • (1990) Neuron , vol.4 , pp. 487-492
    • Rodriguez-Tébar, A.1    Dechant, G.2    Barde, Y.-A.3
  • 43
    • 0026608541 scopus 로고
    • Binding of neurotrophin-3 to its neuronal receptors and interactions with nerve growth factor and brain-derived neurotrophic factor
    • Rodriguez-Tébar, A., Dechant, G., Gotz, R. and Barde, Y.A. (1992) Binding of neurotrophin-3 to its neuronal receptors and interactions with nerve growth factor and brain-derived neurotrophic factor. EMBO J., 11, 917-922.
    • (1992) EMBO J. , vol.11 , pp. 917-922
    • Rodriguez-Tébar, A.1    Dechant, G.2    Gotz, R.3    Barde, Y.A.4
  • 45
    • 0028063876 scopus 로고
    • Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor(1-76) in solution and comparison with the DNA-binding domain of the 434 repressor
    • Sevilla-Sierra, P., Otting, G. and Wüthrich, K. (1994) Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor(1-76) in solution and comparison with the DNA-binding domain of the 434 repressor. J. Mol. Biol., 235, 1003-1020.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1003-1020
    • Sevilla-Sierra, P.1    Otting, G.2    Wüthrich, K.3
  • 46
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • Stanger, B.Z., Leder, P., Lee, T.H., Kim, E. and Seed, B. (1995) RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell, 81, 513-523.
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 47
    • 44049114111 scopus 로고
    • Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets
    • Szyperski, T., Güntert, P., Otting, G. and Wüthrich, K. (1992) Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets. J. Magn. Resonance, 99, 552-560.
    • (1992) J. Magn. Resonance , vol.99 , pp. 552-560
    • Szyperski, T.1    Güntert, P.2    Otting, G.3    Wüthrich, K.4
  • 48
    • 0027275490 scopus 로고
    • A novel domain within the 55 kd TNF receptor signals cell death
    • Tartaglia, L.A., Ayres, T.M., Wong, G.H.W. and Goeddel, D.V. (1993) A novel domain within the 55 kd TNF receptor signals cell death. Cell, 74, 845-853.
    • (1993) Cell , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.W.3    Goeddel, D.V.4
  • 49
    • 0029913681 scopus 로고    scopus 로고
    • A potential mechanism of 'cross-talk' between the p55 tumor necrosis factor receptor and Fas/APO1: Proteins binding to the death domains of the two receptors also bind to each other
    • Varfolomeev, E.E., Boldin, M.P., Goncharov, T.M. and Wallach, D. (1996) A potential mechanism of 'cross-talk' between the p55 tumor necrosis factor receptor and Fas/APO1: proteins binding to the death domains of the two receptors also bind to each other. J. Exp. Med., 183, 1271-1275.
    • (1996) J. Exp. Med. , vol.183 , pp. 1271-1275
    • Varfolomeev, E.E.1    Boldin, M.P.2    Goncharov, T.M.3    Wallach, D.4


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