메뉴 건너뛰기




Volumn 423, Issue 6939, 2003, Pages 555-560

Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; COMPLEXATION; CRYSTAL STRUCTURE; HYDROPHOBICITY; PROTEINS;

EID: 0038526314     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01645     Document Type: Article
Times cited : (493)

References (30)
  • 1
    • 0012473279 scopus 로고
    • The nuclear receptor superfamily: The second decade
    • Mangelsdorf, D. J. et al. The nuclear receptor superfamily: the second decade. Cell 83, 835-839 (1995).
    • (1995) Cell , vol.83 , pp. 835-839
    • Mangelsdorf, D.J.1
  • 2
    • 0033305499 scopus 로고    scopus 로고
    • Orphan nuclear receptors: From gene to function
    • Giguere, V. Orphan nuclear receptors: from gene to function. Endocr. Rev. 20, 689-725 (1999).
    • (1999) Endocr. Rev. , vol.20 , pp. 689-725
    • Giguere, V.1
  • 3
    • 0031833450 scopus 로고    scopus 로고
    • The nuclear receptor ligand-binding domain: Structure and function
    • Moras, D. & Gronemeyer, H. The nuclear receptor ligand-binding domain: structure and function. Curr. Opin. Cell Biol. 10, 384-391 (1998).
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 384-391
    • Moras, D.1    Gronemeyer, H.2
  • 4
    • 0035976638 scopus 로고    scopus 로고
    • Nuclear receptors and lipid physiology: Opening the X-files
    • Chawla, A., Repa, J. J., Evans, R. M. & Mangelsdorf, D. J. Nuclear receptors and lipid physiology: opening the X-files. Science 294, 1866-1870 (2001).
    • (2001) Science , vol.294 , pp. 1866-1870
    • Chawla, A.1    Repa, J.J.2    Evans, R.M.3    Mangelsdorf, D.J.4
  • 5
    • 0033617520 scopus 로고    scopus 로고
    • Orphan nuclear receptors: Shifting endocrinology into reverse
    • Kliewer, S. A., Lehmann, J. M. & Willson, T. M. Orphan nuclear receptors: shifting endocrinology into reverse. Science 284, 757-760 (1999).
    • (1999) Science , vol.284 , pp. 757-760
    • Kliewer, S.A.1    Lehmann, J.M.2    Willson, T.M.3
  • 6
    • 0036710140 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor 4 is a transcription factor that constitutively binds fatty acids
    • Wisely, G. B. et al. Hepatocyte nuclear factor 4 is a transcription factor that constitutively binds fatty acids. Structure 10, 1225-1234 (2002).
    • (2002) Structure , vol.10 , pp. 1225-1234
    • Wisely, G.B.1
  • 7
    • 0037063997 scopus 로고    scopus 로고
    • Crystal structure of the HNF4α ligand binding domain in complex with endogenous fatty acid ligand
    • Dhe-Paganon, S., Duda, K., Iwamoto, M., Chi, Y. I. & Shoelson, S. E. Crystal structure of the HNF4α ligand binding domain in complex with endogenous fatty acid ligand. J. Biol. Chem. 277, 37973-37976 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 37973-37976
    • Dhe-Paganon, S.1    Duda, K.2    Iwamoto, M.3    Chi, Y.I.4    Shoelson, S.E.5
  • 8
    • 0027074637 scopus 로고
    • Identification of a new brain-specific transcription factor, NURR1
    • Law, S. W., Conneely, O. M., DeMayo, F. J. & O'Malley, B. W. Identification of a new brain-specific transcription factor, NURR1. Mol. Endocrinol. 6, 2129-2135 (1992).
    • (1992) Mol. Endocrinol. , vol.6 , pp. 2129-2135
    • Law, S.W.1    Conneely, O.M.2    DeMayo, F.J.3    O'Malley, B.W.4
  • 9
    • 0031002024 scopus 로고    scopus 로고
    • Dopamine neuron agenesis in Nurr1-deficient mice
    • Zetterstrom, R. H. et al. Dopamine neuron agenesis in Nurr1-deficient mice. Science 276, 248-250 (1997).
    • (1997) Science , vol.276 , pp. 248-250
    • Zetterstrom, R.H.1
  • 10
    • 0032584085 scopus 로고    scopus 로고
    • Nurr1 is essential for the induction of the dopaminergic phenotype and the survival of ventral mesencephalic late dopaminergic precursor neurons
    • Saucedo-Cardenas, O. et al. Nurr1 is essential for the induction of the dopaminergic phenotype and the survival of ventral mesencephalic late dopaminergic precursor neurons. Proc. Natl Acad. Sci. USA 95, 4013-4018 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4013-4018
    • Saucedo-Cardenas, O.1
  • 11
    • 0037226797 scopus 로고    scopus 로고
    • Mutations in NR4A2 associated with familial Parkinson disease
    • Le, W. D. et al. Mutations in NR4A2 associated with familial Parkinson disease. Nature Genet. 33, 85-89 (2003).
    • (2003) Nature Genet. , vol.33 , pp. 85-89
    • Le, W.D.1
  • 12
    • 0033601290 scopus 로고    scopus 로고
    • Activity of the Nurr1 carboxylterminal domain depends on cell type and integrity of the activation function 2
    • Castro, D. S., Arvidsson, M., Bondesson Bolin, M. & Perlmann, T. Activity of the Nurr1 carboxylterminal domain depends on cell type and integrity of the activation function 2. J. Biol. Chem. 274, 37483-37490 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 37483-37490
    • Castro, D.S.1    Arvidsson, M.2    Bondesson Bolin, M.3    Perlmann, T.4
  • 13
    • 0030056997 scopus 로고    scopus 로고
    • A canonical structure for the ligand-binding domain of nuclear receptors
    • Wurtz, J. M. et al. A canonical structure for the ligand-binding domain of nuclear receptors. Nature Struct. Biol. 3, 87-94 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 87-94
    • Wurtz, J.M.1
  • 14
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
    • Renaud, J. P. et al. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378, 681-689 (1995).
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.P.1
  • 15
    • 0030667676 scopus 로고    scopus 로고
    • Molecular basis of agonism and antagonism in the oestrogen receptor
    • Brzozowski, A. M. et al. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature 389, 753-758 (1997).
    • (1997) Nature , vol.389 , pp. 753-758
    • Brzozowski, A.M.1
  • 16
    • 0032505096 scopus 로고    scopus 로고
    • Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ
    • Nolte, R. T. et al. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ. Nature 395, 137-143 (1998).
    • (1998) Nature , vol.395 , pp. 137-143
    • Nolte, R.T.1
  • 17
    • 0036187372 scopus 로고    scopus 로고
    • Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3
    • Greschik, H. et al. Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol. Cell 9, 303-313 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 303-313
    • Greschik, H.1
  • 18
    • 0031866761 scopus 로고    scopus 로고
    • The NGFI-B subfamily of the nuclear receptor superfamily
    • Maruyama, K. et al. The NGFI-B subfamily of the nuclear receptor superfamily. Int. J. Oncol. 12, 1237-1243 (1998).
    • (1998) Int. J. Oncol. , vol.12 , pp. 1237-1243
    • Maruyama, K.1
  • 19
    • 0032213219 scopus 로고    scopus 로고
    • Structure and specificity of nuclear receptor-coactivator interactions
    • Darimont, B. D. et al. Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev. 12, 3343-3356 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3343-3356
    • Darimont, B.D.1
  • 20
    • 0033637850 scopus 로고    scopus 로고
    • Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding
    • Pissios, P., Tzameli, I., Kushner, P. & Moore, D. D. Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding. Mol. Cell 6, 245-253 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 245-253
    • Pissios, P.1    Tzameli, I.2    Kushner, P.3    Moore, D.D.4
  • 21
    • 0037144591 scopus 로고    scopus 로고
    • Defining requirements for heterodimerization between the retinoid X receptor and the orphan nuclear receptor Nurr 1
    • Aarnisalo, P., Kim, C. H., Lee, J. W. & Perlmann, T. Defining requirements for heterodimerization between the retinoid X receptor and the orphan nuclear receptor Nurr1. J. Biol. Chem. 277, 35118-35123 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 35118-35123
    • Aarnisalo, P.1    Kim, C.H.2    Lee, J.W.3    Perlmann, T.4
  • 22
    • 0031451570 scopus 로고    scopus 로고
    • Evolution of the nuclear receptor superfamily: Early diversification from an ancestral orphan receptor
    • Laudet, V. Evolution of the nuclear receptor superfamily: early diversification from an ancestral orphan receptor. J. Mol. Endocrinol. 19, 207-226 (1997).
    • (1997) J. Mol. Endocrinol. , vol.19 , pp. 207-226
    • Laudet, V.1
  • 23
    • 0030962710 scopus 로고    scopus 로고
    • Ligand binding was acquired during evolution of nuclear receptors
    • Escriva, H. et al. Ligand binding was acquired during evolution of nuclear receptors. Proc. Natl Acad. Sci. USA 94, 6803-6808 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6803-6808
    • Escriva, H.1
  • 24
    • 0036787839 scopus 로고    scopus 로고
    • Phosphorylation and intramolecular stabilization of the ligand binding domain in the nuclear receptor steroidogenic factor 1
    • Desclozeaux, M., Krylova, I. N., Horn, F., Fletterick, R. J. & Ingraham, H. A. Phosphorylation and intramolecular stabilization of the ligand binding domain in the nuclear receptor steroidogenic factor 1. Mol. Cell. Biol. 22, 7193-7203 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7193-7203
    • Desclozeaux, M.1    Krylova, I.N.2    Horn, F.3    Fletterick, R.J.4    Ingraham, H.A.5
  • 25
    • 0034465598 scopus 로고    scopus 로고
    • Structure-function analysis of the Rev-erbA and RVR ligand-binding domains reveals a large hydrophobic surface that mediates corepressor binding and a ligand cavity occupied by side chains
    • Renaud, J. P., Harris, J. M., Downes, M., Burke, L. J. & Muscat, G. E. Structure-function analysis of the Rev-erbA and RVR ligand-binding domains reveals a large hydrophobic surface that mediates corepressor binding and a ligand cavity occupied by side chains. Mol. Endocrinol. 14, 700-717 (2000).
    • (2000) Mol. Endocrinol. , vol.14 , pp. 700-717
    • Renaud, J.P.1    Harris, J.M.2    Downes, M.3    Burke, L.J.4    Muscat, G.E.5
  • 26
    • 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 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 28
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • De la Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De la Fortelle, E.1    Bricogne, G.2
  • 29
    • 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
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.