메뉴 건너뛰기




Volumn 10, Issue 6, 1999, Pages 550-556

Ligand-binding domain of estrogen receptors

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; ESTROGEN RECEPTOR; LIGAND; MUTANT PROTEIN; RECEPTOR SUBTYPE; REPRESSOR PROTEIN;

EID: 0032728389     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(99)00034-8     Document Type: Review
Times cited : (36)

References (50)
  • 1
    • 0030031782 scopus 로고    scopus 로고
    • Estrogen receptors: Bioactivities and interaction with cell signaling pathways
    • Katzenellenbogen B.S. Estrogen receptors: bioactivities and interaction with cell signaling pathways. Biol Reprod. 54:1996;287-293.
    • (1996) Biol Reprod , vol.54 , pp. 287-293
    • Katzenellenbogen, B.S.1
  • 2
    • 0028919090 scopus 로고
    • Estrogen receptors in human nontarget tissues: Biological and clinical implications
    • Ciocca D.R., Roig L.M. Estrogen receptors in human nontarget tissues: biological and clinical implications. Endocrinol Rev. 16:1995;35-62.
    • (1995) Endocrinol Rev , vol.16 , pp. 35-62
    • Ciocca, D.R.1    Roig, L.M.2
  • 3
    • 0031833450 scopus 로고    scopus 로고
    • The nuclear receptor ligand-binding domain: Structure and function
    • The authors give an overview of different nuclear receptor ligand-binding domains structures in a condensed form. The most relevant information on co-activators/co-repressors is also presented.
    • Moras D., Gronemeyer H. The nuclear receptor ligand-binding domain: structure and function. Curr Opin Cell Biol. 10:1998;384-391. The authors give an overview of different nuclear receptor ligand-binding domains structures in a condensed form. The most relevant information on co-activators/co-repressors is also presented.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 384-391
    • Moras, D.1    Gronemeyer, H.2
  • 5
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tannenbaum D.M., Wang Y., Williams S.P., Sigler P.B. Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci USA. 95:1998;5998-6003.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5998-6003
    • Tannenbaum, D.M.1    Wang, Y.2    Williams, S.P.3    Sigler, P.B.4
  • 6
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • The first example of a crystal structure of a ternary complex of the hERα ligand-binding domain (LBD) in complex with an agonist (diethylstilbestrol) and a co-activator fragment. The crystal structure of the hER LBD in complex with a partial agonist, tamoxifen, is also presented. The structural basis for co-activator recognition is also discussed with respect to the interaction of tamoxifen with the protein.
    • Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., Greene G.L. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell. 95:1998;927-937. The first example of a crystal structure of a ternary complex of the hERα ligand-binding domain (LBD) in complex with an agonist (diethylstilbestrol) and a co-activator fragment. The crystal structure of the hER LBD in complex with a partial agonist, tamoxifen, is also presented. The structural basis for co-activator recognition is also discussed with respect to the interaction of tamoxifen with the protein.
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6    Greene, G.L.7
  • 8
    • 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. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature. 375:1995;377-382.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 9
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid
    • Renaud J.P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., Moras D. Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature. 378:1995;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
  • 12
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • Williams S.P., Sigler P.B. Atomic structure of progesterone complexed with its receptor. Nature. 393:1998;392-396.
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 17
    • 0023857147 scopus 로고
    • Identification of a new class of steroid hormone receptors
    • Giguere V., Yang N., Segui P., Evans R.M. Identification of a new class of steroid hormone receptors. Nature. 331:1988;91-94.
    • (1988) Nature , vol.331 , pp. 91-94
    • Giguere, V.1    Yang, N.2    Segui, P.3    Evans, R.M.4
  • 18
    • 0031736649 scopus 로고    scopus 로고
    • Oestrogen receptor beta (ERβ)
    • Saunders P. Oestrogen receptor beta (ERβ). Rev Reprod. 3:1998;164-171.
    • (1998) Rev Reprod , vol.3 , pp. 164-171
    • Saunders, P.1
  • 20
    • 0031975052 scopus 로고    scopus 로고
    • Espression of estrogen receptor beta messenger RNA variant in breast cancer
    • Vladusik E.A., Hornby A.E., Guerra Vladusik F.K., Lupu R. Espression of estrogen receptor beta messenger RNA variant in breast cancer. Cancer Res. 58:1998;210-214.
    • (1998) Cancer Res , vol.58 , pp. 210-214
    • Vladusik, E.A.1    Hornby, A.E.2    Guerra Vladusik, F.K.3    Lupu, R.4
  • 21
    • 0031791153 scopus 로고    scopus 로고
    • Identification of estrogen receptor β2, a functional variant of estrogen receptor β expressed in normal rat tissues
    • Petersen D.N., Tkalcevic G.T., Koza-Taylor P.H., Turi T.G., Brown T.A. Identification of estrogen receptor β2, a functional variant of estrogen receptor β expressed in normal rat tissues. Endocrinology. 139:1998;1082-1092.
    • (1998) Endocrinology , vol.139 , pp. 1082-1092
    • Petersen, D.N.1    Tkalcevic, G.T.2    Koza-Taylor, P.H.3    Turi, T.G.4    Brown, T.A.5
  • 22
    • 0032495993 scopus 로고    scopus 로고
    • Novel isoform of rat estrogen receptor beta with 18 amino acid insertion in the ligand binding domain as a putative dominant negative regulator of estrogen action
    • Maruyama K., Endoh H., Sasaki-Iwaoka H., Kanou H., Shimaya E., Hashimoto S., Kato S., Kawashima H.A. novel isoform of rat estrogen receptor beta with 18 amino acid insertion in the ligand binding domain as a putative dominant negative regulator of estrogen action. Biochem Biophys Res Commun. 246:1998;142-147.
    • (1998) Biochem Biophys Res Commun , vol.246 , pp. 142-147
    • Maruyama, K.1    Endoh, H.2    Sasaki-Iwaoka, H.3    Kanou, H.4    Shimaya, E.5    Hashimoto, S.6    Kato, S.7    Kawashima, H.A.8
  • 24
    • 0032893084 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999
    • Bairoch A., Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999. Nucleic Acid Res. 27:1999;49-54.
    • (1999) Nucleic Acid Res , vol.27 , pp. 49-54
    • Bairoch, A.1    Apweiler, R.2
  • 25
    • 0031059270 scopus 로고    scopus 로고
    • The estradiol pharmacophore: Ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site
    • Anstead G.M., Carlson K.E., Katzenellenbogen J.A. The estradiol pharmacophore: ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site. Steroids. 62:1997;268-303.
    • (1997) Steroids , vol.62 , pp. 268-303
    • Anstead, G.M.1    Carlson, K.E.2    Katzenellenbogen, J.A.3
  • 26
    • 0032554879 scopus 로고    scopus 로고
    • Three dimensional models of estrogen receptor ligand binding domain complexes, based on related crystal structures and mutational and structure-activity relationship data
    • Thorough comparative modelling study. The hERα ligand-binding domain (LBD) model is evaluated based on the analysis of ligands and their relative binding affinities. The article provides a list of mutants within the LBD of human and mouse estrogen receptor evaluating the binding affinities with respect to the wild-type receptor.
    • Wurtz J.M., Egner U., Heinrich N., Moras D., Mueller-Fahrnow A. Three dimensional models of estrogen receptor ligand binding domain complexes, based on related crystal structures and mutational and structure-activity relationship data. J Med Chem. 11:1998;1803-1814. Thorough comparative modelling study. The hERα ligand-binding domain (LBD) model is evaluated based on the analysis of ligands and their relative binding affinities. The article provides a list of mutants within the LBD of human and mouse estrogen receptor evaluating the binding affinities with respect to the wild-type receptor.
    • (1998) J Med Chem , vol.11 , pp. 1803-1814
    • Wurtz, J.M.1    Egner, U.2    Heinrich, N.3    Moras, D.4    Mueller-Fahrnow, A.5
  • 28
    • 0031888317 scopus 로고    scopus 로고
    • Selective estrogen receptor modulators (SERMs)
    • Grese T.A., Dodge J.A. Selective estrogen receptor modulators (SERMs). Curr Pharmaceut Des. 4:1998;71-92.
    • (1998) Curr Pharmaceut des , vol.4 , pp. 71-92
    • Grese, T.A.1    Dodge, J.A.2
  • 29
    • 2642593030 scopus 로고    scopus 로고
    • The key to antiestrogenic mechanism of raloxifene is amino acid 351 (aspartate) in the estrogen receptor
    • Levenson A.S., Jordan V.C. The key to antiestrogenic mechanism of raloxifene is amino acid 351 (aspartate) in the estrogen receptor. Cancer Res. 58:1998;1872-1875.
    • (1998) Cancer Res , vol.58 , pp. 1872-1875
    • Levenson, A.S.1    Jordan, V.C.2
  • 30
    • 0031778177 scopus 로고    scopus 로고
    • Basic guide to the mechanism of antiestrogen action
    • Macgregor J.I., Jordan V.C. Basic guide to the mechanism of antiestrogen action. Pharmacol Rev. 50:1998;151-196.
    • (1998) Pharmacol Rev , vol.50 , pp. 151-196
    • Macgregor, J.I.1    Jordan, V.C.2
  • 31
    • 0004752110 scopus 로고    scopus 로고
    • Novel ligands that function as selective estrogens or antiestrogens for estrogen receptor-α Or estrogen receptor-β
    • Sun J., Meyers M.J., Fink B.E., Rajendran R., Katzenellenbogen J.A., Katzenellenbogen B.S. Novel ligands that function as selective estrogens or antiestrogens for estrogen receptor-α or estrogen receptor-β Endocrinology. 140:1999;800-804.
    • (1999) Endocrinology , vol.140 , pp. 800-804
    • Sun, J.1    Meyers, M.J.2    Fink, B.E.3    Rajendran, R.4    Katzenellenbogen, J.A.5    Katzenellenbogen, B.S.6
  • 32
    • 0033096995 scopus 로고    scopus 로고
    • Comparative QSAR analysis of estrogen receptor ligands
    • This study provides detailed information on comparative structure-activity relationships of steroidal and non-steroidal estrogen receptor ligands. Factors influencing the relative binding affinity, for example, the steric and polar character of substituents are highlighted. The quality of the derived relationships is critically analysed.
    • Gao H., Katzenellenbogen J.A., Garg R., Hansch C. Comparative QSAR analysis of estrogen receptor ligands. Chem Rev. 99:1999;723-744. This study provides detailed information on comparative structure-activity relationships of steroidal and non-steroidal estrogen receptor ligands. Factors influencing the relative binding affinity, for example, the steric and polar character of substituents are highlighted. The quality of the derived relationships is critically analysed.
    • (1999) Chem Rev , vol.99 , pp. 723-744
    • Gao, H.1    Katzenellenbogen, J.A.2    Garg, R.3    Hansch, C.4
  • 33
    • 0032526951 scopus 로고    scopus 로고
    • Two distinct nuclear receptor interaction domains in NSD1, a novel SET protein that exhibits characteristics of both corepressors and coactivators
    • Huang N., von Baur E., Garnier J.M., Lerouge T., Vonesch J.L., Lutz Y., Chambon P., Losson R. Two distinct nuclear receptor interaction domains in NSD1, a novel SET protein that exhibits characteristics of both corepressors and coactivators. EMBO J. 17:1998;3398-3412.
    • (1998) EMBO J , vol.17 , pp. 3398-3412
    • Huang, N.1    Von Baur, E.2    Garnier, J.M.3    Lerouge, T.4    Vonesch, J.L.5    Lutz, Y.6    Chambon, P.7    Losson, R.8
  • 34
    • 0032079794 scopus 로고    scopus 로고
    • The yeast Ada complex mediates the ligand-dependent activation function AF-2 of retinoid X and estrogen receptors
    • vom Baur E., Harbers M., Um S.J., Benecke A., Chambon P., Losson R. The yeast Ada complex mediates the ligand-dependent activation function AF-2 of retinoid X and estrogen receptors. Genes Dev. 12:1998;1278-1289.
    • (1998) Genes Dev , vol.12 , pp. 1278-1289
    • Vom Baur, E.1    Harbers, M.2    Um, S.J.3    Benecke, A.4    Chambon, P.5    Losson, R.6
  • 35
    • 0032951135 scopus 로고    scopus 로고
    • The orphan nuclear receptor SHP inhibits agonist-dependent transcriptional activation of estrogen receptors ERα and ERβ
    • Johansson L., Thomsen J.S., Damdimopoulos A.E., Spyrou G., Gustafsson J.A., Treuter E. The orphan nuclear receptor SHP inhibits agonist-dependent transcriptional activation of estrogen receptors ERα and ERβ J Biol Chem. 274:1999;345-353.
    • (1999) J Biol Chem , vol.274 , pp. 345-353
    • Johansson, L.1    Thomsen, J.S.2    Damdimopoulos, A.E.3    Spyrou, G.4    Gustafsson, J.A.5    Treuter, E.6
  • 36
    • 0032549531 scopus 로고    scopus 로고
    • Enhancement of estrogen receptor transcriptional activity by the coactivator GRIP-1 highlights the role of activation function 2 in determining estrogen receptor pharmacology
    • The authors analyze the interaction of the co-activator GRIP1 with the estrogen receptor. They suggest that GRIP1 may not only interact with the transactivation function 2 (AF-2) of the ligand-binding domain (LBD) but also contacts the receptor in yet unidentified areas of the LBD. The results are supported by mutagenesis experiments of selected amino acid residues in helix H12 of the LBD.
    • Norris J.D., Fan D., Stallcup M.R., McDonnell D.P. Enhancement of estrogen receptor transcriptional activity by the coactivator GRIP-1 highlights the role of activation function 2 in determining estrogen receptor pharmacology. J Biol Chem. 273:1998;6679-6688. The authors analyze the interaction of the co-activator GRIP1 with the estrogen receptor. They suggest that GRIP1 may not only interact with the transactivation function 2 (AF-2) of the ligand-binding domain (LBD) but also contacts the receptor in yet unidentified areas of the LBD. The results are supported by mutagenesis experiments of selected amino acid residues in helix H12 of the LBD.
    • (1998) J Biol Chem , vol.273 , pp. 6679-6688
    • Norris, J.D.1    Fan, D.2    Stallcup, M.R.3    McDonnell, D.P.4
  • 37
    • 0032961682 scopus 로고    scopus 로고
    • Estrogen receptor domains E and F: Role in dimerisation and interaction with coactivator RIP-140
    • Peters G.A., Khan S.A. Estrogen receptor domains E and F: role in dimerisation and interaction with coactivator RIP-140. Mol Endocrinol. 13:1999;286-296.
    • (1999) Mol Endocrinol , vol.13 , pp. 286-296
    • Peters, G.A.1    Khan, S.A.2
  • 38
    • 0031611355 scopus 로고    scopus 로고
    • Transcriptional activation by oestrogen receptors
    • Parker M.G. Transcriptional activation by oestrogen receptors. Biochem Soc Symp. 63:1998;45-50.
    • (1998) Biochem Soc Symp , vol.63 , pp. 45-50
    • Parker, M.G.1
  • 39
    • 0030946198 scopus 로고    scopus 로고
    • Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen
    • Smith C.L., Nawaz Z., O'Malley B.W. Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol Endocrinol. 11:1997;657-666.
    • (1997) Mol Endocrinol , vol.11 , pp. 657-666
    • Smith, C.L.1    Nawaz, Z.2    O'Malley, B.W.3
  • 41
    • 0031936094 scopus 로고    scopus 로고
    • Estrogen receptor mutations and changes in estrogen receptor and progesterone receptor protein expression in metastatic or recurrent breast cancer
    • Umekita Y., Sagara Y., Yoshida H. Estrogen receptor mutations and changes in estrogen receptor and progesterone receptor protein expression in metastatic or recurrent breast cancer. Jpn J Cancer Res. 89:1998;27-32.
    • (1998) Jpn J Cancer Res , vol.89 , pp. 27-32
    • Umekita, Y.1    Sagara, Y.2    Yoshida, H.3
  • 42
    • 0032472911 scopus 로고    scopus 로고
    • Different positioning of the ligand-binding domain helix 12 and the F domain of the estrogen receptor accounts for functional differences between agonists and antagonists
    • Nichols M., Rientjes J.M.J., Stewart A.F. Different positioning of the ligand-binding domain helix 12 and the F domain of the estrogen receptor accounts for functional differences between agonists and antagonists. EMBO J. 17:1998;765-773.
    • (1998) EMBO J , vol.17 , pp. 765-773
    • Nichols, M.1    Rientjes, J.M.J.2    Stewart, A.F.3
  • 43
    • 0031974628 scopus 로고    scopus 로고
    • Determinants of ligand binding specificity of estrogen receptor-α: Estrogen versus androgen discrimination
    • Ekena K., Katzenellenbogen J.A., Katzenellenbogen B.S. Determinants of ligand binding specificity of estrogen receptor-α: estrogen versus androgen discrimination. J Biol Chem. 273:1998;693-699.
    • (1998) J Biol Chem , vol.273 , pp. 693-699
    • Ekena, K.1    Katzenellenbogen, J.A.2    Katzenellenbogen, B.S.3
  • 44
    • 0032031082 scopus 로고    scopus 로고
    • Ligand-independent activation of the estrogen receptors α and β by mutations of a conserved tyrosine can be abolished by antiestrogens
    • Tremblay G.B., Tremblay A., Labrie F., Giguère V. Ligand-independent activation of the estrogen receptors α and β by mutations of a conserved tyrosine can be abolished by antiestrogens. Cancer Res. 58:1998;877-881.
    • (1998) Cancer Res , vol.58 , pp. 877-881
    • Tremblay, G.B.1    Tremblay, A.2    Labrie, F.3    Giguère, V.4
  • 45
    • 0033053616 scopus 로고    scopus 로고
    • Dominant activity of activation function 1 (AF-1) and differential stoichiometric requirements for AF-1 and-2 in the estrogen receptor α-β heterodimeric complex
    • Tremblay G.B., Tremblay A., Labrie F., Giguère V. Dominant activity of activation function 1 (AF-1) and differential stoichiometric requirements for AF-1 and-2 in the estrogen receptor α-β heterodimeric complex. Mol Cell Biol. 19:1999;1919-1927.
    • (1999) Mol Cell Biol , vol.19 , pp. 1919-1927
    • Tremblay, G.B.1    Tremblay, A.2    Labrie, F.3    Giguère, V.4
  • 48
    • 0031941755 scopus 로고    scopus 로고
    • Random mutagenesis of human estrogen receptor ligand binding domain identifies mutations that decrease sensitivity to estradiol and increase sensitivity to a diphenol indene-ol compound: Basis for a regulatable expression system
    • Miller N., Whelan J. Random mutagenesis of human estrogen receptor ligand binding domain identifies mutations that decrease sensitivity to estradiol and increase sensitivity to a diphenol indene-ol compound: basis for a regulatable expression system. J Steroid Biochem Mol Biol. 64:1998;129-135.
    • (1998) J Steroid Biochem Mol Biol , vol.64 , pp. 129-135
    • Miller, N.1    Whelan, J.2
  • 49
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acid Res. 22:1994;4673-4680.
    • (1994) Nucleic Acid Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 50
    • 85031619317 scopus 로고    scopus 로고
    • Insight98.0. San Diego, USA: MSI Inc.
    • Insight98.0. San Diego, USA: MSI Inc.; 1998.
    • (1998)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.