메뉴 건너뛰기




Volumn 70, Issue , 2014, Pages 21-36

Architecture of DNA bound RAR heterodimers

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; LIGAND; RETINOIC ACID; RETINOIC ACID RECEPTOR; RETINOID X RECEPTOR; RETINOL;

EID: 84910118219     PISSN: 03060225     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-94-017-9050-5_2     Document Type: Article
Times cited : (10)

References (61)
  • 1
    • 36549078554 scopus 로고    scopus 로고
    • Dynamics of coactivator recruitment and chromatin modifications during nuclear receptor mediated transcription
    • Aoyagi S, Archer TK (2008) Dynamics of coactivator recruitment and chromatin modifications during nuclear receptor mediated transcription. Mol Cell Endo 280:1-5
    • (2008) Mol Cell Endo , vol.280 , pp. 1-5
    • Aoyagi, S.1    Archer, T.K.2
  • 2
    • 25644452125 scopus 로고    scopus 로고
    • A robust characterization of retinoic acid response elements based on a comparison of sites in three species
    • Balmer JE, Blomhoff R (2005) A robust characterization of retinoic acid response elements based on a comparison of sites in three species. J Steroid Biochem Mol Biol 96:347-354
    • (2005) J Steroid Biochem Mol Biol , vol.96 , pp. 347-354
    • Balmer, J.E.1    Blomhoff, R.2
  • 4
    • 84879086561 scopus 로고    scopus 로고
    • Allosteric controls of nuclear receptor function in the regulation of transcription
    • Billas I, Moras D (2013) Allosteric controls of nuclear receptor function in the regulation of transcription. J Mol Biol 425:2317-2329
    • (2013) J Mol Biol , vol.425 , pp. 2317-2329
    • Billas, I.1    Moras, D.2
  • 5
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha
    • Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D (1995) Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature 375:377-382
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 6
    • 0033868825 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains
    • Bourguet W, Vivat V, Wurtz JM, Chambon P, Gronemeyer H, Moras D (2000) Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol Cell 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
  • 8
    • 84875363845 scopus 로고    scopus 로고
    • Multidomain integration in the structure of the HNF-4alpha nuclear receptor complex
    • Chandra V, Huang P, Potluri N, Wu D, Kim Y, Rastinejad F (2013) Multidomain integration in the structure of the HNF-4alpha nuclear receptor complex. Nature 495:394-398
    • (2013) Nature , vol.495 , pp. 394-398
    • Chandra, V.1    Huang, P.2    Potluri, N.3    Wu, D.4    Kim, Y.5    Rastinejad, F.6
  • 9
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • Cramer P, Bushnell DA, Kornberg RD (2001) Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 292:1863-1876
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 10
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer J, Epp O, Miki K, Huber R, Michel H (1984) X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol 180:385-398
    • (1984) J Mol Biol , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 12
    • 0034213831 scopus 로고    scopus 로고
    • Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid
    • Egea PF, Mitschler A, Rochel N, Ruff M, Chambon P, Moras D (2000) Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid. EMBO J 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
  • 13
    • 0037050017 scopus 로고    scopus 로고
    • Co-regulator recruitment and the mechanism of retinoic acid receptor synergy
    • Germain P, Iyer J, Zechel C, Gronemeyer H (2002) Co-regulator recruitment and the mechanism of retinoic acid receptor synergy. Nature 415:187-192
    • (2002) Nature , vol.415 , pp. 187-192
    • Germain, P.1    Iyer, J.2    Zechel, C.3    Gronemeyer, H.4
  • 15
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG (2000) The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 14:121-141
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 16
    • 84867508210 scopus 로고    scopus 로고
    • Validation of macromolecular flexibility in solution by small-angle X-ray scattering (SAXS)
    • Hammel M (2012) Validation of macromolecular flexibility in solution by small-angle X-ray scattering (SAXS). Eur Biophys J 41:789-799
    • (2012) Eur Biophys J , vol.41 , pp. 789-799
    • Hammel, M.1
  • 17
    • 84884914684 scopus 로고    scopus 로고
    • Looking at nuclear receptors from a new angle
    • Helsen C, Claessens F (2013) Looking at nuclear receptors from a new angle. Mol Cell Endocrinol 382:97-106
    • (2013) Mol Cell Endocrinol , vol.382 , pp. 97-106
    • Helsen, C.1    Claessens, F.2
  • 18
    • 67549104319 scopus 로고    scopus 로고
    • Genomic antagonism between retinoic acid and estrogen signaling in breast cancer
    • Hua S, Kittler R, White KP (2009) Genomic antagonism between retinoic acid and estrogen signaling in breast cancer. Cell 137:1259-1271
    • (2009) Cell , vol.137 , pp. 1259-1271
    • Hua, S.1    Kittler, R.2    White, K.P.3
  • 19
    • 78649324289 scopus 로고    scopus 로고
    • Structural and functional insights into nuclear receptor signaling
    • Jin L, Li Y (2010) Structural and functional insights into nuclear receptor signaling. Adv Drug Deliv Rev 62:1218-1226
    • (2010) Adv Drug Deliv Rev , vol.62 , pp. 1218-1226
    • Jin, L.1    Li, Y.2
  • 20
    • 0029947425 scopus 로고    scopus 로고
    • Individual subunits of heterodimers comprised of retinoic acid and retinoid X receptors interact with their ligands independently
    • Kersten S, Dawson MI, Lewis BA, Noy N (1996) Individual subunits of heterodimers comprised of retinoic acid and retinoid X receptors interact with their ligands independently. Biochemistry 35:3816-3824
    • (1996) Biochemistry , vol.35 , pp. 3816-3824
    • Kersten, S.1    Dawson, M.I.2    Lewis, B.A.3    Noy, N.4
  • 22
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann L, Pan J, Liu YH (2011) Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem Soc Rev 40:1224-1234
    • (2011) Chem Soc Rev , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.H.3
  • 25
    • 84866607246 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Modulators of pathology and therapeutic targets
    • Lonard DM, O'Malley BW (2012) Nuclear receptor coregulators: modulators of pathology and therapeutic targets. Nat Rev Endocrinol 8:598-604
    • (2012) Nat Rev Endocrinol , vol.8 , pp. 598-604
    • Lonard, D.M.1    O'Malley, B.W.2
  • 27
    • 0027381438 scopus 로고
    • The patterns of binding of RAR, RXR and TR homo- and heterodimers to direct repeats are dictated by the binding specificites of the DNA binding domains
    • Mader S, Chen JY, Chen Z, White J, Chambon P, Gronemeyer H (1993) The patterns of binding of RAR, RXR and TR homo- and heterodimers to direct repeats are dictated by the binding specificites of the DNA binding domains. EMBO J 12:5029-5041
    • (1993) EMBO J , vol.12 , pp. 5029-5041
    • Mader, S.1    Chen, J.Y.2    Chen, Z.3    White, J.4    Chambon, P.5    Gronemeyer, H.6
  • 29
    • 79958250822 scopus 로고    scopus 로고
    • Genome-wide interplay of nuclear receptors with the epigenome
    • Martens JH, Rao NA, Stunnenberg HG (2011) Genome-wide interplay of nuclear receptors with the epigenome. Biochim Biophys Acta 1812:818-823
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 818-823
    • Martens, J.H.1    Rao, N.A.2    Stunnenberg, H.G.3
  • 30
    • 82655173855 scopus 로고    scopus 로고
    • Nuclear hormone receptors: Allosteric switches
    • McEwan IJ (2012) Nuclear hormone receptors: allosteric switches. Mol Cell Endocrinol 348:345-347
    • (2012) Mol Cell Endocrinol , vol.348 , pp. 345-347
    • McEwan, I.J.1
  • 31
    • 34249667205 scopus 로고    scopus 로고
    • Natural disordered sequences in the amino terminal domain of nuclear receptors: Lessons from the androgen and glucocorticoid receptors
    • McEwan IJ, Lavery D, Fischer K, Watt K (2007) Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors. Nucl Recept Signal 5:e001
    • (2007) Nucl Recept Signal , vol.5
    • McEwan, I.J.1    Lavery, D.2    Fischer, K.3    Watt, K.4
  • 32
    • 65249167505 scopus 로고    scopus 로고
    • DNA binding site sequence directs glucocorticoid receptor structure and activity
    • Meijsing SH, Pufall MA, So AY, Bates DL, Chen L, Yamamoto KR (2009) DNA binding site sequence directs glucocorticoid receptor structure and activity. Science 324:407-410
    • (2009) Science , vol.324 , pp. 407-410
    • Meijsing, S.H.1    Pufall, M.A.2    So, A.Y.3    Bates, D.L.4    Chen, L.5    Yamamoto, K.R.6
  • 36
    • 84857183093 scopus 로고    scopus 로고
    • Structure of the full human RXR/VDR nuclear receptor heterodimer complex with its DR3 target DNA
    • Orlov I, Rochel N, Moras D, Klaholz BP (2012) Structure of the full human RXR/VDR nuclear receptor heterodimer complex with its DR3 target DNA. EMBO J 31:291-300
    • (2012) EMBO J , vol.31 , pp. 291-300
    • Orlov, I.1    Rochel, N.2    Moras, D.3    Klaholz, B.P.4
  • 39
    • 84857776910 scopus 로고    scopus 로고
    • General molecular biology and architecture of nuclear receptors
    • Pawlak M, Lefebvre P, Staels B (2012) General molecular biology and architecture of nuclear receptors. Curr Top Med Chem 12:486-504
    • (2012) Curr Top Med Chem , vol.12 , pp. 486-504
    • Pawlak, M.1    Lefebvre, P.2    Staels, B.3
  • 40
    • 21744435965 scopus 로고    scopus 로고
    • Controlling nuclear receptors: The circular logic of cofactor cycles
    • Perissi V, Rosenfeld MG (2005) Controlling nuclear receptors: the circular logic of cofactor cycles. Nat Rev Mol Cell Biol 6:542-554
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 542-554
    • Perissi, V.1    Rosenfeld, M.G.2
  • 41
    • 0027237598 scopus 로고
    • Determinants for selective RAR and TR recognition of direct repeat HREs
    • Perlmann T, Rangarajan PN, Umesono K, Evans RM (1993) Determinants for selective RAR and TR recognition of direct repeat HREs. Genes Dev 7:1411-1422
    • (1993) Genes Dev , vol.7 , pp. 1411-1422
    • Perlmann, T.1    Rangarajan, P.N.2    Umesono, K.3    Evans, R.M.4
  • 42
    • 19944430311 scopus 로고    scopus 로고
    • Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies
    • Pogenberg V, Guichou JF, Vivat-Hannah V, Kammerer S, Pérez E, Germain P, de Lera AR, Gronemeyer H, Royer CA, Bourguet W (2005) Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies. J Biol Chem 280:1625-1633
    • (2005) J Biol Chem , vol.280 , pp. 1625-1633
    • Pogenberg, V.1    Guichou, J.F.2    Vivat-Hannah, V.3    Kammerer, S.4    Pérez, E.5    Germain, P.6    de Lera, A.R.7    Gronemeyer, H.8    Royer, C.A.9    Bourguet, W.10
  • 43
    • 69249090970 scopus 로고    scopus 로고
    • Direct interdomain interactions can mediate allosterism in the thyroid receptor
    • Putcha BD, Fernandez EJ (2009) Direct interdomain interactions can mediate allosterism in the thyroid receptor. J Biol Chem 284:22517-22524
    • (2009) J Biol Chem , vol.284 , pp. 22517-22524
    • Putcha, B.D.1    Fernandez, E.J.2
  • 44
    • 84877778935 scopus 로고    scopus 로고
    • Super-resolution in solution x-ray scattering and its applications to structural systems biology
    • Rambo RP, Tainer JA (2013) Super-resolution in solution x-ray scattering and its applications to structural systems biology. Annu Rev Biophys. 42:415-441
    • (2013) Annu Rev Biophys , vol.42 , pp. 415-441
    • Rambo, R.P.1    Tainer, J.A.2
  • 45
    • 0034161266 scopus 로고    scopus 로고
    • Structure of the RXR-RAR DNAbinding complex on the retinoic acid response element DR1
    • Rastinejad F, Wagner T, Zhao Q, Khorasanizadeh S (2000) Structure of the RXR-RAR DNAbinding complex on the retinoic acid response element DR1. EMBO J 19:1045-1054
    • (2000) EMBO J , vol.19 , pp. 1045-1054
    • Rastinejad, F.1    Wagner, T.2    Zhao, Q.3    Khorasanizadeh, S.4
  • 46
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid
    • Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D (1995) Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature 378:681-689
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.P.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 49
    • 0024392753 scopus 로고
    • Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution
    • Rould MA, Perona JJ, Söll D, Steitz TA (1989) Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution. Science 246:1135-1142
    • (1989) Science , vol.246 , pp. 1135-1142
    • Rould, M.A.1    Perona, J.J.2    Söll, D.3    Steitz, T.A.4
  • 51
    • 79952103416 scopus 로고    scopus 로고
    • Negative regulation by nuclear receptors: A plethora of mechanisms
    • Santos GM, Fairall L, Schwabe JW (2011) Negative regulation by nuclear receptors: a plethora of mechanisms. Trends Endocrinol Metab 22:87-93
    • (2011) Trends Endocrinol Metab , vol.22 , pp. 87-93
    • Santos, G.M.1    Fairall, L.2    Schwabe, J.W.3
  • 53
    • 0031043055 scopus 로고    scopus 로고
    • The phantom ligand effect: Allosteric control of transcription by the retinoid X receptor
    • Schulman IG, Li C, Schwabe JW, Evans RM (1997) The phantom ligand effect: allosteric control of transcription by the retinoid X receptor. Genes Dev 11:299-308
    • (1997) Genes Dev , vol.11 , pp. 299-308
    • Schulman, I.G.1    Li, C.2    Schwabe, J.W.3    Evans, R.M.4
  • 54
    • 0025223160 scopus 로고
    • Solution structure of the DNA-binding domain of the oestrogen receptor
    • Schwabe JW, Neuhaus D, Rhodes D (1990) Solution structure of the DNA-binding domain of the oestrogen receptor. Nature 348(6300):458-461
    • (1990) Nature , vol.348 , Issue.6300 , pp. 458-461
    • Schwabe, J.W.1    Neuhaus, D.2    Rhodes, D.3
  • 55
    • 0034614372 scopus 로고    scopus 로고
    • Crystal versus solution structures of thiamine diphosphate-dependent enzymes
    • Svergun DI, Petoukhov MV, Koch MH, König S (2000) Crystal versus solution structures of thiamine diphosphate-dependent enzymes. J Biol Chem 275:297-302
    • (2000) J Biol Chem , vol.275 , pp. 297-302
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3    König, S.4
  • 56
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MH (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys J 80:2946-2953
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.