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Volumn 399, Issue 1, 2010, Pages 120-132

X-Ray structures of the LXRα LBD in its homodimeric form and implications for heterodimer signaling

Author keywords

Cholesterol; Crystal; GW3965; Helix 12; Interface

Indexed keywords

3 CHLORO 4 [3 (7 PROPYL 3 TRIFLUOROMETHYLBENZISOXAZOL 6 YLOXY)PROPYLTHIO]PHENYLACETIC ACID; 3 [3 [[2 CHLORO 3 (TRIFLUOROMETHYL)BENZYL](2 DIPHENYLETHYL)AMINO]PROPOXY]PHENYLACETIC ACID; BENZISOXAZOLE DERIVATIVE; BENZISOXAZOLE UREA; GW 9365; LIVER X RECEPTOR AGONIST; LIVER X RECEPTOR ALPHA; LIVER X RECEPTOR BETA; STEROID RECEPTOR COACTIVATOR 1; UNCLASSIFIED DRUG;

EID: 77953083339     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.04.005     Document Type: Article
Times cited : (50)

References (46)
  • 1
    • 47949094965 scopus 로고    scopus 로고
    • Integration of metabolism and inflammation by lipid-activated nuclear receptors
    • Bensinger J.S., Tontonoz P. Integration of metabolism and inflammation by lipid-activated nuclear receptors. Nature 2008, 454:470-477.
    • (2008) Nature , vol.454 , pp. 470-477
    • Bensinger, J.S.1    Tontonoz, P.2
  • 3
    • 18144440415 scopus 로고    scopus 로고
    • A novel liver X receptor agonist established species differences in the regulation of cholesterol 7α-hydroxylase (CYP7a)
    • Menke J.G., Macnaul K.L., Hayes N.S., Baffic J., Chao Y.S., Elbrecht A., et al. A novel liver X receptor agonist established species differences in the regulation of cholesterol 7α-hydroxylase (CYP7a). Endocrinology 2002, 143:2548-2558.
    • (2002) Endocrinology , vol.143 , pp. 2548-2558
    • Menke, J.G.1    Macnaul, K.L.2    Hayes, N.S.3    Baffic, J.4    Chao, Y.S.5    Elbrecht, A.6
  • 4
    • 23444431623 scopus 로고    scopus 로고
    • Retinoid X receptor heterodimers in the metabolic syndrome
    • Shulman A.I., Mangelsdorf D.J. Retinoid X receptor heterodimers in the metabolic syndrome. N. Engl. J. Med. 2005, 353:604-615.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 604-615
    • Shulman, A.I.1    Mangelsdorf, D.J.2
  • 5
    • 46149098344 scopus 로고    scopus 로고
    • LXR signaling couples sterol metabolism to proliferation in the acquired immune response
    • Bensinger J.S., Bradley M.N., Joseph S.B., Zelcer N., Janssen E.M., Hausner M.A., et al. LXR signaling couples sterol metabolism to proliferation in the acquired immune response. Cell 2008, 134:97-111.
    • (2008) Cell , vol.134 , pp. 97-111
    • Bensinger, J.S.1    Bradley, M.N.2    Joseph, S.B.3    Zelcer, N.4    Janssen, E.M.5    Hausner, M.A.6
  • 6
    • 1542573353 scopus 로고    scopus 로고
    • Structure-activity relationship of nuclear receptor ligand interactions
    • Greschik H., Moras D. Structure-activity relationship of nuclear receptor ligand interactions. Curr. Top. Med. Chem. 2003, 3:1573-1599.
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 1573-1599
    • Greschik, H.1    Moras, D.2
  • 8
    • 39049136131 scopus 로고    scopus 로고
    • Design, structure-activity relationships and X-ray cocrystallography of non-steroidal LXR agonists
    • Bennett D.J., Carswell E.J., Cooke A.J., Edwards A.S., Nimz O. Design, structure-activity relationships and X-ray cocrystallography of non-steroidal LXR agonists. Curr. Med. Chem. 2008, 15:195-209.
    • (2008) Curr. Med. Chem. , vol.15 , pp. 195-209
    • Bennett, D.J.1    Carswell, E.J.2    Cooke, A.J.3    Edwards, A.S.4    Nimz, O.5
  • 10
    • 0033681001 scopus 로고    scopus 로고
    • Asymmetry in the PPARγ/RXRα crystal structure reveals the molecular basis of heterodimerization among nuclear receptors
    • Gampe R.T., Montana V.G., Lambert M.H., Miller A.B., Bledsoe R.K., Milburn M.V., et al. Asymmetry in the PPARγ/RXRα crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol. Cell 2000, 5:545-555.
    • (2000) Mol. Cell , vol.5 , pp. 545-555
    • Gampe, R.T.1    Montana, V.G.2    Lambert, M.H.3    Miller, A.B.4    Bledsoe, R.K.5    Milburn, M.V.6
  • 11
    • 0038012478 scopus 로고    scopus 로고
    • Identification of a novel set of genes regulated by a unique liver X receptor-alpha;-mediated transcription mechanism
    • Anderson L.M., Choe S.E., Yukhananov R.Y., Hopfner R.L., Church G.M., Pratt R.E., Dzau V.J. Identification of a novel set of genes regulated by a unique liver X receptor-α-mediated transcription mechanism. J. Biol. Chem. 2003, 278:15252-15260.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15252-15260
    • Anderson, L.M.1    Choe, S.E.2    Yukhananov, R.Y.3    Hopfner, R.L.4    Church, G.M.5    Pratt, R.E.6    Dzau, V.J.7
  • 12
    • 70349581877 scopus 로고    scopus 로고
    • Rexinoid bexarotene modulates triglyceride but not cholesterol metabolism via gene-specific permissivity of the RXR/LXR heterodimer in the liver
    • Lalloyer F., Pedersen T.Å., Gross B., Lestavel S., Yous S., Vallez E., et al. Rexinoid bexarotene modulates triglyceride but not cholesterol metabolism via gene-specific permissivity of the RXR/LXR heterodimer in the liver. Arterioscler., Thromb., Vasc. Biol. 2009, 29:1488-1495.
    • (2009) Arterioscler., Thromb., Vasc. Biol. , vol.29 , pp. 1488-1495
    • Lalloyer, F.1    Pedersen, T.Å.2    Gross, B.3    Lestavel, S.4    Yous, S.5    Vallez, E.6
  • 13
  • 14
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf D.J., Evans R.M. The RXR heterodimers and orphan receptors. Cell 1995, 83:841-850.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 15
    • 1642304065 scopus 로고    scopus 로고
    • Structural determinants of allosteric ligand activation in RXR heterodimers
    • Shulman A.I., Larson C., Mangelsdorf D.J., Ranganathan R. Structural determinants of allosteric ligand activation in RXR heterodimers. Cell 2004, 116:417-429.
    • (2004) Cell , vol.116 , pp. 417-429
    • Shulman, A.I.1    Larson, C.2    Mangelsdorf, D.J.3    Ranganathan, R.4
  • 16
    • 0033868825 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric complex of RAR and RXR ligand binding domains
    • Bourguet W., Vivat V., Wurtz J.M., Chambon P., Gronemeyer H., Moras D. Crystal structure of a heterodimeric complex of RAR and RXR ligand binding domains. Mol. Cell 2000, 5:289-298.
    • (2000) Mol. Cell , vol.5 , pp. 289-298
    • Bourguet, W.1    Vivat, V.2    Wurtz, J.M.3    Chambon, P.4    Gronemeyer, H.5    Moras, D.6
  • 17
    • 0032505066 scopus 로고    scopus 로고
    • Interactions controlling the assembly of nuclear receptor heterodimers and co-activators
    • Westin S., Kurokawa R., Nolte R.T., Wisely G.B., McInervey E.M., Rose D.W., et al. Interactions controlling the assembly of nuclear receptor heterodimers and co-activators. Nature 1998, 395:199-202.
    • (1998) Nature , vol.395 , pp. 199-202
    • Westin, S.1    Kurokawa, R.2    Nolte, R.T.3    Wisely, G.B.4    McInervey, E.M.5    Rose, D.W.6
  • 18
    • 0142223221 scopus 로고    scopus 로고
    • The three-dimensional structure of the liver X receptor β reveals a flexible ligand-binding pocket that can accommodate fundamentally different ligands
    • Färnegårdh M., Bonn T., Sun S., Ljunggren J., Ahola H., Wilhelmsson A., et al. The three-dimensional structure of the liver X receptor β reveals a flexible ligand-binding pocket that can accommodate fundamentally different ligands. J. Biol. Chem. 2003, 278:38821-38828.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38821-38828
    • Färnegårdh, M.1    Bonn, T.2    Sun, S.3    Ljunggren, J.4    Ahola, H.5    Wilhelmsson, A.6
  • 19
    • 0345304733 scopus 로고    scopus 로고
    • Crystal structure of the human liver X receptor β ligand binding domain in complex with a synthetic agonist
    • Hoerer S., Schmid A., Heckel A., Budzinski R.M., Nar H. Crystal structure of the human liver X receptor β ligand binding domain in complex with a synthetic agonist. J. Mol. Biol. 2003, 334:853-861.
    • (2003) J. Mol. Biol. , vol.334 , pp. 853-861
    • Hoerer, S.1    Schmid, A.2    Heckel, A.3    Budzinski, R.M.4    Nar, H.5
  • 20
    • 23944439351 scopus 로고    scopus 로고
    • Discovery of substituted maleimides as liver X receptor agonists and determination of a ligand-bound crystal structure
    • Jaye M.C., Krawiec J.A., Campobasso N., Smallwood A., Qiu C., Lu Q., et al. Discovery of substituted maleimides as liver X receptor agonists and determination of a ligand-bound crystal structure. J. Med. Chem. 2005, 48:5419-5422.
    • (2005) J. Med. Chem. , vol.48 , pp. 5419-5422
    • Jaye, M.C.1    Krawiec, J.A.2    Campobasso, N.3    Smallwood, A.4    Qiu, C.5    Lu, Q.6
  • 22
    • 0141737105 scopus 로고    scopus 로고
    • Crystal structure of the heterodimeric complex of LXRα and RXRβ ligand-binding domains in a fully agonistic conformation
    • Svensson S., Ostberg T., Jacobsson M., Norstrom M., Stefansson K., Hallen D., et al. Crystal structure of the heterodimeric complex of LXRα and RXRβ ligand-binding domains in a fully agonistic conformation. EMBO J. 2003, 22:4625-4633.
    • (2003) EMBO J. , vol.22 , pp. 4625-4633
    • Svensson, S.1    Ostberg, T.2    Jacobsson, M.3    Norstrom, M.4    Stefansson, K.5    Hallen, D.6
  • 27
    • 0037046543 scopus 로고    scopus 로고
    • Identification of a nonsteroidal liver X receptor agonist through parallel array synthesis of tertiary amines
    • Collins J.L., Fivush A.M., Watson M.A., Galardi C.M., Lewis M.C., Moore L.B., et al. Identification of a nonsteroidal liver X receptor agonist through parallel array synthesis of tertiary amines. J. Med. Chem. 2002, 45:1963-1966.
    • (2002) J. Med. Chem. , vol.45 , pp. 1963-1966
    • Collins, J.L.1    Fivush, A.M.2    Watson, M.A.3    Galardi, C.M.4    Lewis, M.C.5    Moore, L.B.6
  • 28
    • 30444447387 scopus 로고    scopus 로고
    • Different role of liver X receptor α and β in lipid metabolism: effects of an α-selective and a dual agonist in mice deficient in each subtype
    • Lund E.G., Peterson L.B., Adams A.D., Lam M.N., Burton C.A., Chin J., et al. Different role of liver X receptor α and β in lipid metabolism: effects of an α-selective and a dual agonist in mice deficient in each subtype. Biochem. Pharmacol. 2006, 71:453-463.
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 453-463
    • Lund, E.G.1    Peterson, L.B.2    Adams, A.D.3    Lam, M.N.4    Burton, C.A.5    Chin, J.6
  • 29
    • 33847366561 scopus 로고    scopus 로고
    • Substituted 2-[(4-aminomethyl)-2-methylpropionic acid PPARα agonists. 1. Discovery of a novel series of potent HDLc raising agents
    • Sierra M.L., Beneton V., Boullay A.B., Boyer T., Brewster A.G., Donche F., et al. Substituted 2-[(4-aminomethyl)-2-methylpropionic acid PPARα agonists. 1. Discovery of a novel series of potent HDLc raising agents. J. Med. Chem. 2007, 50:685-695.
    • (2007) J. Med. Chem. , vol.50 , pp. 685-695
    • Sierra, M.L.1    Beneton, V.2    Boullay, A.B.3    Boyer, T.4    Brewster, A.G.5    Donche, F.6
  • 30
    • 0038752647 scopus 로고    scopus 로고
    • Structural basis for bile acid binding and activation of the nuclear receptor FXR
    • Mi L.Z., Devarakonda S., Harp J.M., Han Q., Pellicciari R., Willson T.M., et al. Structural basis for bile acid binding and activation of the nuclear receptor FXR. Mol. Cell 2003, 4:1093-1100.
    • (2003) Mol. Cell , vol.4 , pp. 1093-1100
    • Mi, L.Z.1    Devarakonda, S.2    Harp, J.M.3    Han, Q.4    Pellicciari, R.5    Willson, T.M.6
  • 31
    • 0043168030 scopus 로고    scopus 로고
    • Coactivator binding promotes the specific interaction between ligand and the pregnane X receptor
    • Watkins R.E., Davis-Searles P.R.D., Lambert M.H., Redinbo M.R. Coactivator binding promotes the specific interaction between ligand and the pregnane X receptor. J. Mol. Biol. 2003, 331:815-828.
    • (2003) J. Mol. Biol. , vol.331 , pp. 815-828
    • Watkins, R.E.1    Davis-Searles, P.R.D.2    Lambert, M.H.3    Redinbo, M.R.4
  • 32
    • 0034213831 scopus 로고    scopus 로고
    • Crystal structure of the human RXRα ligand binding domain bound to its natural ligand:9-cis-retinoic acid
    • Egea P.F., Mitschler A., Rochel N., Ruff M., Chambon P., Moras D. Crystal structure of the human RXRα ligand binding domain bound to its natural ligand:9-cis-retinoic acid. EMBO J. 2000, 19:2592-2601.
    • (2000) EMBO J. , vol.19 , pp. 2592-2601
    • Egea, P.F.1    Mitschler, A.2    Rochel, N.3    Ruff, M.4    Chambon, P.5    Moras, D.6
  • 33
    • 0037204724 scopus 로고    scopus 로고
    • Connections and regulation of the human estrogen receptor
    • McDonnell D.P., Norris J.D. Connections and regulation of the human estrogen receptor. Science 2002, 296:1642-1644.
    • (2002) Science , vol.296 , pp. 1642-1644
    • McDonnell, D.P.1    Norris, J.D.2
  • 34
    • 0031042762 scopus 로고    scopus 로고
    • Unique requirements for retinoid-dependent transcriptional activation by the orphan receptor LXR
    • Willy P., Mangelsdorf D.J. Unique requirements for retinoid-dependent transcriptional activation by the orphan receptor LXR. Genes Dev. 1997, 11:289-298.
    • (1997) Genes Dev. , vol.11 , pp. 289-298
    • Willy, P.1    Mangelsdorf, D.J.2
  • 36
    • 33646204900 scopus 로고    scopus 로고
    • A novel principle for partial agonism of liver X receptor ligands. Competitive recruitment of activators and repressors
    • Albers M., Blume B., Schlueter T., Wright M.B., Kober I., Kremoser C., et al. A novel principle for partial agonism of liver X receptor ligands. Competitive recruitment of activators and repressors. J. Biol. Chem. 2006, 281:4920-4930.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4920-4930
    • Albers, M.1    Blume, B.2    Schlueter, T.3    Wright, M.B.4    Kober, I.5    Kremoser, C.6
  • 37
    • 38549097071 scopus 로고    scopus 로고
    • The universal protein resource (UniProt)
    • UniProt Consortium
    • The universal protein resource (UniProt). Nucleic Acids Res. 2008, 36:D190-D195. UniProt Consortium.
    • (2008) Nucleic Acids Res. , vol.36
  • 38
    • 0033855471 scopus 로고    scopus 로고
    • Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix
    • Gampe R.T., Montana V.G., Lambert M.H. Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix. Genes Dev. 2000, 14:2229-2241.
    • (2000) Genes Dev. , vol.14 , pp. 2229-2241
    • Gampe, R.T.1    Montana, V.G.2    Lambert, M.H.3
  • 39
    • 0032505096 scopus 로고    scopus 로고
    • Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ
    • Nolte R.T., Wisely G.B., Westin S., Cobb J.E., Lambert M.H., Kurokawa R., et al. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ. Nature 1998, 395:137-143.
    • (1998) Nature , vol.395 , pp. 137-143
    • Nolte, R.T.1    Wisely, G.B.2    Westin, S.3    Cobb, J.E.4    Lambert, M.H.5    Kurokawa, R.6
  • 40
    • 0034791264 scopus 로고    scopus 로고
    • Distinct retinoid X receptor activation function-2 residues mediate transactivation in homodimeric and vitamin D receptor heterodimeric contexts
    • Thompson P.D., Remus L.S., Hsieh J.-C., Jurutka P.W., Whitfield G.K., Galligan M.A., et al. Distinct retinoid X receptor activation function-2 residues mediate transactivation in homodimeric and vitamin D receptor heterodimeric contexts. J. Mol. Endocrinol. 2001, 27:211-227.
    • (2001) J. Mol. Endocrinol. , vol.27 , pp. 211-227
    • Thompson, P.D.1    Remus, L.S.2    Hsieh, J.-C.3    Jurutka, P.W.4    Whitfield, G.K.5    Galligan, M.A.6
  • 41
    • 0035937246 scopus 로고    scopus 로고
    • Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR
    • Egea P.F., Roche N., Birck C., Vachette P., Timmins P.A., Moras D. Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR. J. Mol. Biol. 2001, 307:557-576.
    • (2001) J. Mol. Biol. , vol.307 , pp. 557-576
    • Egea, P.F.1    Roche, N.2    Birck, C.3    Vachette, P.4    Timmins, P.A.5    Moras, D.6
  • 42
    • 40449093255 scopus 로고    scopus 로고
    • RXR heterodimerization allosterically activates LXR binding to the second NR box of activating signal co-integrator-2
    • Son Y., Park O.G., Kim G.S., Lee J.W., Lee Y.C. RXR heterodimerization allosterically activates LXR binding to the second NR box of activating signal co-integrator-2. Biochem. J. 2008, 410:319-330.
    • (2008) Biochem. J. , vol.410 , pp. 319-330
    • Son, Y.1    Park, O.G.2    Kim, G.S.3    Lee, J.W.4    Lee, Y.C.5
  • 43
    • 0034623288 scopus 로고    scopus 로고
    • Sterol-dependent transactivation of the ABC1 promoter by the liver X receptor/retinoid X receptor
    • Costet P., Luo Y., Wang N., Tall A.R. Sterol-dependent transactivation of the ABC1 promoter by the liver X receptor/retinoid X receptor. J. Biol. Chem. 2000, 275:28240-28245.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28240-28245
    • Costet, P.1    Luo, Y.2    Wang, N.3    Tall, A.R.4
  • 44
    • 0033326582 scopus 로고    scopus 로고
    • Ligand independent coregulator recruitment by the triply activatable OR1/retinoid X receptor-α nuclear receptor heterodimer
    • Wiebel F.F., Steffensen K.R., Treuter E., Feltkamp D., Gustafsson J.-Å. Ligand independent coregulator recruitment by the triply activatable OR1/retinoid X receptor-α nuclear receptor heterodimer. Mol. Endocrinol. 1999, 13:1105-1118.
    • (1999) Mol. Endocrinol. , vol.13 , pp. 1105-1118
    • Wiebel, F.F.1    Steffensen, K.R.2    Treuter, E.3    Feltkamp, D.4    Gustafsson, J.-Å.5
  • 46
    • 52449127472 scopus 로고    scopus 로고
    • Structure-guided design of N-phenyl tertiary amines as transrepression-selective liver X receptor modulators with anti-inflammatory activity
    • Chao E.Y., Caravella J.A., Watson M.A., Campobasso N., Ghisletti S., Billin A.N., et al. Structure-guided design of N-phenyl tertiary amines as transrepression-selective liver X receptor modulators with anti-inflammatory activity. J. Med. Chem. 2008, 51:5758-5765.
    • (2008) J. Med. Chem. , vol.51 , pp. 5758-5765
    • Chao, E.Y.1    Caravella, J.A.2    Watson, M.A.3    Campobasso, N.4    Ghisletti, S.5    Billin, A.N.6


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