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Volumn 10, Issue 2, 2003, Pages 136-140

A dynamic mechanism of nuclear receptor activation and its perturbation in a human disease

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; LIGAND; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; TRANSCRIPTION FACTOR;

EID: 0037317303     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb892     Document Type: Article
Times cited : (146)

References (33)
  • 1
    • 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
  • 2
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau, A.K. et al. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95, 927-937 (1998).
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1
  • 3
    • 0032505096 scopus 로고    scopus 로고
    • Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor
    • Nolte, R. et al. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor. Nature 395, 137-143 (1998).
    • (1998) Nature , vol.395 , pp. 137-143
    • Nolte, R.1
  • 4
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet, W., Ruff, M., Chambon, R., Gronemeyer, H., & Moras, D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 375, 377-382 (1995).
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, R.3    Gronemeyer, H.4    Moras, D.5
  • 5
    • 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
  • 6
    • 0033198735 scopus 로고    scopus 로고
    • Structure of the ligand-binding domain of oestrogen receptor βε in the presence of a partial agonist and a full antagonist
    • Pike, A.C. et al. Structure of the ligand-binding domain of oestrogen receptor βε in the presence of a partial agonist and a full antagonist. EMBO J. 18, 4608-4618 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4608-4618
    • Pike, A.C.1
  • 7
    • 0033855471 scopus 로고    scopus 로고
    • Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix
    • Gampe, R.T. Jr. et al. Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix. Genes Dev. 14, 2229-2241 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 2229-2241
    • Gampe R.T., Jr.1
  • 8
    • 0033868825 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains
    • Bourguet, W. et al. Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol. Cell 5, 289-298 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 289-298
    • Bourguet, W.1
  • 9
    • 0035099225 scopus 로고    scopus 로고
    • Structural insights into the mode of action of a pure antiestrogen
    • Pike, A.C. et al. Structural insights into the mode of action of a pure antiestrogen. Structure 9, 145-153 (2001).
    • (2001) Structure , vol.9 , pp. 145-153
    • Pike, A.C.1
  • 10
    • 0035933511 scopus 로고    scopus 로고
    • The human nuclear xenobiotic receptor PXR: Structural determinants of directed promiscuity
    • Watkins, R.E. et al. The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. Science 292, 2329-2333 (2001).
    • (2001) Science , vol.292 , pp. 2329-2333
    • Watkins, R.E.1
  • 11
    • 0035852767 scopus 로고    scopus 로고
    • The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation
    • Clayton, G.M., Peak-Chew, S.Y., Evans, R.M., & Schwabe, J.W. The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation. Proc. Natl. Acad. Sci. USA 98, 1549-1554 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1549-1554
    • Clayton, G.M.1    Peak-Chew, S.Y.2    Evans, R.M.3    Schwabe, J.W.4
  • 12
    • 18244393501 scopus 로고    scopus 로고
    • Structural basis for antagonist-mediated recruitment of nuclear corepressors by PPARα
    • Xu, H.E. et al. Structural basis for antagonist-mediated recruitment of nuclear corepressors by PPARα. Nature 415, 813-817 (2002).
    • (2002) Nature , vol.415 , pp. 813-817
    • Xu, H.E.1
  • 13
    • 0033523917 scopus 로고    scopus 로고
    • The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors
    • Hu, X., & Lazar, M.A. The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature 402, 93-96 (1999).
    • (1999) Nature , vol.402 , pp. 93-96
    • Hu, X.1    Lazar, M.A.2
  • 14
    • 0033572656 scopus 로고    scopus 로고
    • Molecular determinants of nuclear receptor-corepressor interaction
    • Perissi, V. et al. Molecular determinants of nuclear receptor-corepressor interaction. Genes Dev. 13, 3198-3208 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 3198-3208
    • Perissi, V.1
  • 15
    • 17544398986 scopus 로고    scopus 로고
    • Mechanism of corepressor binding and release from nuclear hormone receptors
    • Nagy, L. et al. Mechanism of corepressor binding and release from nuclear hormone receptors. Genes Dev. 13, 3209-3216 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 3209-3216
    • Nagy, L.1
  • 16
    • 0034536085 scopus 로고    scopus 로고
    • The nuclear receptor corepressor (N-CoR) contains three isoleucine motifs (I/LXXII) that serve as receptor interaction domains (IDs)
    • Webb, P. et al. The nuclear receptor corepressor (N-CoR) contains three isoleucine motifs (I/LXXII) that serve as receptor interaction domains (IDs). Mol. Endocrinol. 14, 1976-1985 (2000).
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1976-1985
    • Webb, P.1
  • 17
    • 0033599038 scopus 로고    scopus 로고
    • Dominant negative mutations in human PPARγ associated with severe insulin resistance, diabetes mellitus and hypertension
    • Barroso, I. et al. Dominant negative mutations in human PPARγ associated with severe insulin resistance, diabetes mellitus and hypertension. Nature 402, 880-883 (1999).
    • (1999) Nature , vol.402 , pp. 880-883
    • Barroso, I.1
  • 18
    • 17744415288 scopus 로고    scopus 로고
    • Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element
    • Chong, S. et al. Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene 192, 271-281 (1997).
    • (1997) Gene , vol.192 , pp. 271-281
    • Chong, S.1
  • 19
    • 0029016829 scopus 로고
    • An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor γ (PPARγ)
    • Lehmann, J.M. et al. An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor γ (PPARγ). J. Biol. Chem. 270, 12953-12956 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12953-12956
    • Lehmann, J.M.1
  • 20
    • 0014829630 scopus 로고
    • Segmental flexibility in an antibody molecule
    • Yguerabide, J., Epstein, H.F., & Stryer, L. Segmental flexibility in an antibody molecule. J. Mol. Biol. 51, 573-590 (1970).
    • (1970) J. Mol. Biol. , vol.51 , pp. 573-590
    • Yguerabide, J.1    Epstein, H.F.2    Stryer, L.3
  • 21
    • 0034646179 scopus 로고    scopus 로고
    • Backbone dynamics of Tet repressor α8-α9 loop
    • Verganl, B. et al. Backbone dynamics of Tet repressor α8-α9 loop. Biochemistry 39, 2759-2768 (2000).
    • (2000) Biochemistry , vol.39 , pp. 2759-2768
    • Verganl, B.1
  • 22
    • 0032578423 scopus 로고    scopus 로고
    • Backbone flexibility of five sites on the catalytic subunit of cAMP-dependent protein kinase in the open and closed conformations
    • Gangal, M. et al. Backbone flexibility of five sites on the catalytic subunit of cAMP-dependent protein kinase in the open and closed conformations. Biochemistry 37, 13728-13735 (1998).
    • (1998) Biochemistry , vol.37 , pp. 13728-13735
    • Gangal, M.1
  • 23
    • 0037172819 scopus 로고    scopus 로고
    • Light-induced changes in the structure and accessibility of the cytoplasmic loops of rhodopsin in the activated MII state
    • Mielke, T., Alexiev, U., Glasel, M., Otto, H., & Heyn, M.P. Light-induced changes in the structure and accessibility of the cytoplasmic loops of rhodopsin in the activated MII state. Biochemistry 41, 7875-7884 (2002).
    • (2002) Biochemistry , vol.41 , pp. 7875-7884
    • Mielke, T.1    Alexiev, U.2    Glasel, M.3    Otto, H.4    Heyn, M.P.5
  • 25
    • 0034724560 scopus 로고    scopus 로고
    • Ligand-induced stabilization of PPARγ monitored by NMR spectroscopy: Implications for nuclear receptor activation
    • Johnson, B.A. et al. Ligand-induced stabilization of PPARγ monitored by NMR spectroscopy: implications for nuclear receptor activation. J. Mol. Biol. 298, 187-194 (2000).
    • (2000) J. Mol. Biol. , vol.298 , pp. 187-194
    • Johnson, B.A.1
  • 26
    • 0035431321 scopus 로고    scopus 로고
    • Structure of the PPARα and -γ ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family
    • Cronet, P. et al. Structure of the PPARα and -γ ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family. Structure 9, 699-706 (2001).
    • (2001) Structure , vol.9 , pp. 699-706
    • Cronet, P.1
  • 27
    • 0035805514 scopus 로고    scopus 로고
    • Crystal structure of a mutant hERα ligand-binding domain reveals key structural features for the mechanism of partial agonism
    • Gangloff, M. et al. Crystal structure of a mutant hERα ligand-binding domain reveals key structural features for the mechanism of partial agonism. J. Biol. Chem. 276, 15059-15065 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 15059-15065
    • Gangloff, M.1
  • 28
    • 0029938795 scopus 로고    scopus 로고
    • Activation and repression by nuclear hormone receptors: Hormone modulates an equilibrium between active and repressive states
    • Schulman, I.G., Juguilon, H., & Evans, R.M. Activation and repression by nuclear hormone receptors: hormone modulates an equilibrium between active and repressive states. Mol. Cell. Biol. 16, 3807-3813 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3807-3813
    • Schulman, I.G.1    Juguilon, H.2    Evans, R.M.3
  • 29
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tanenbaum, D.M., Wang, Y., Williams, S.R & Sigler, P.B. Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc. Natl. Acad. Sci. USA 95, 5998-6003 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5998-6003
    • Tanenbaum, D.M.1    Wang, Y.2    Williams, S.R.3    Sigler, P.B.4
  • 30
    • 0037192817 scopus 로고    scopus 로고
    • The structural basis for the specificity of retinoid-X-receptor selective agonists: New insights into the role of helix H12
    • Love, J.D. et al. The structural basis for the specificity of retinoid-X-receptor selective agonists: new insights into the role of helix H12. J. Biol. Chem. 277, 11385-11391 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 11385-11391
    • Love, J.D.1
  • 32
    • 0032989265 scopus 로고    scopus 로고
    • A novel N-aryl tyrosine activator of peroxisome proliferator-activated receptor-γ reverses the diabetic phenotype of the Zucker diabetic fatty rat
    • Brown, K.K. et al. A novel N-aryl tyrosine activator of peroxisome proliferator-activated receptor-γ reverses the diabetic phenotype of the Zucker diabetic fatty rat. Diabetes 48, 1415-1424 (1999).
    • (1999) Diabetes , vol.48 , pp. 1415-1424
    • Brown, K.K.1
  • 33
    • 0036306530 scopus 로고    scopus 로고
    • Evidence for an internal entropy contribution to phosphoryl transfer: A study of domain closure, backbone flexibility, and the catalytic cycle of cAMP-dependent protein kinase
    • Li, F. et al. Evidence for an internal entropy contribution to phosphoryl transfer: a study of domain closure, backbone flexibility, and the catalytic cycle of cAMP-dependent protein kinase. J. Mol. Biol. 315, 459-469 (2002).
    • (2002) J. Mol. Biol. , vol.315 , pp. 459-469
    • Li, F.1


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