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Erschienen in: Breast Cancer Research 5/2000

01.10.2000 | Review

Estrogen receptor transcription and transactivation Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors

verfasst von: Marc Ruff, Monique Gangloff, Jean Marie Wurtz, Dino Moras

Erschienen in: Breast Cancer Research | Ausgabe 5/2000

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Abstract

Estrogen receptors are members of the nuclear receptor steroid family that exhibit specific structural features, ligand-binding domain sequence identity and dimeric interactions, that single them out. The crystal structures of their DNA-binding domains give some insight into how nuclear receptors discriminate between DNA response elements. The various ligand-binding domain crystal structures of the two known estrogen receptor isotypes (α and β) allow one to interpret ligand specificity and reveal the interactions responsible for stabilizing the activation helix H12 in the agonist and antagonist positions.
Literatur
1.
Zurück zum Zitat Walter P, Green S, Greene G, Krust A, Bornert JM, Jeltsch JM, Staub A, Jensen E, Scrace G, Waterfield M, et al: Cloning of the human estrogen receptor cDNA. Proc Natl Acad Sci USA. 1985, 82: 7889-7893.CrossRefPubMedPubMedCentral Walter P, Green S, Greene G, Krust A, Bornert JM, Jeltsch JM, Staub A, Jensen E, Scrace G, Waterfield M, et al: Cloning of the human estrogen receptor cDNA. Proc Natl Acad Sci USA. 1985, 82: 7889-7893.CrossRefPubMedPubMedCentral
2.
Zurück zum Zitat Green S, Walter P, Kumar V, Krust A, Bornert JM, Argos P, Chambon P: Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature. 1986, 320: 134-139.CrossRefPubMed Green S, Walter P, Kumar V, Krust A, Bornert JM, Argos P, Chambon P: Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature. 1986, 320: 134-139.CrossRefPubMed
3.
Zurück zum Zitat Muramatsu M, Inoue S: Estrogen receptors: how do they control reproductive and non reproductive functions?. Biochem Biophys Res Commun. 2000, 270: 1-10. 10.1006/bbrc.2000.2214.CrossRefPubMed Muramatsu M, Inoue S: Estrogen receptors: how do they control reproductive and non reproductive functions?. Biochem Biophys Res Commun. 2000, 270: 1-10. 10.1006/bbrc.2000.2214.CrossRefPubMed
4.
Zurück zum Zitat Ogawa S, Inoue S, Watanabe T, Hiroi H, Orimo A, Hosoi T, Ouchi Y, Muramatsu M: The complete primary structure of human estrogen receptor beta (hER beta) and its heterodimerization with ER alpha in vivo and in vitro. Biochem Biophys Res Commun. 1998, 243: 122-126. 10.1006/bbrc.1997.7893.CrossRefPubMed Ogawa S, Inoue S, Watanabe T, Hiroi H, Orimo A, Hosoi T, Ouchi Y, Muramatsu M: The complete primary structure of human estrogen receptor beta (hER beta) and its heterodimerization with ER alpha in vivo and in vitro. Biochem Biophys Res Commun. 1998, 243: 122-126. 10.1006/bbrc.1997.7893.CrossRefPubMed
5.
Zurück zum Zitat Kuiper GG, Carlsson B, Grandien K, Enmark E, Haggblad J, Nilsson S, Gustafsson JA: Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors alpha and beta. Endocrinology. 1997, 138: 863-870. 10.1210/en.138.3.863.PubMed Kuiper GG, Carlsson B, Grandien K, Enmark E, Haggblad J, Nilsson S, Gustafsson JA: Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors alpha and beta. Endocrinology. 1997, 138: 863-870. 10.1210/en.138.3.863.PubMed
6.
Zurück zum Zitat Luisi BF, Xu WX, Otwinowski Z, Freedman LP, Yamamoto KR, Sigler PB: Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature. 1991, 352: 497-505. 10.1038/352497a0.CrossRefPubMed Luisi BF, Xu WX, Otwinowski Z, Freedman LP, Yamamoto KR, Sigler PB: Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature. 1991, 352: 497-505. 10.1038/352497a0.CrossRefPubMed
7.
Zurück zum Zitat Schwabe JW, Neuhaus D, Rhodes D: Solution structure of the DNA-binding domain of the oestrogen receptor. Nature. 1990, 348: 458-461. 10.1038/348458a0., This study shows the importance of the spacing between the half sites for specific binding on the response elementCrossRefPubMed Schwabe JW, Neuhaus D, Rhodes D: Solution structure of the DNA-binding domain of the oestrogen receptor. Nature. 1990, 348: 458-461. 10.1038/348458a0., This study shows the importance of the spacing between the half sites for specific binding on the response elementCrossRefPubMed
8.
Zurück zum Zitat Schwabe JW, Chapman L, Finch JT, Rhodes D: The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell. 1993, 75: 567-578., This study reveals how the DBD recognizes its own half site sequence response element rather than that of the related glucocorticoid receptor, which differs by only two base pairsCrossRefPubMed Schwabe JW, Chapman L, Finch JT, Rhodes D: The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell. 1993, 75: 567-578., This study reveals how the DBD recognizes its own half site sequence response element rather than that of the related glucocorticoid receptor, which differs by only two base pairsCrossRefPubMed
9.
Zurück zum Zitat Schwabe JW, Chapman L, Rhodes D: The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation. Structure. 1995, 3: 201-213.CrossRefPubMed Schwabe JW, Chapman L, Rhodes D: The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation. Structure. 1995, 3: 201-213.CrossRefPubMed
10.
Zurück zum Zitat Schwabe JW, Chapman L, Finch JT, Rhodes D, Neuhaus D: DNA recognition by the oestrogen receptor: from solution to the crystal. Curr Biol. 1993, 1: 187-204. Schwabe JW, Chapman L, Finch JT, Rhodes D, Neuhaus D: DNA recognition by the oestrogen receptor: from solution to the crystal. Curr Biol. 1993, 1: 187-204.
11.
Zurück zum Zitat Gewirth DT, Sigler PB: The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex. Nat Struct Biol. 1995, 2: 386-394.CrossRefPubMed Gewirth DT, Sigler PB: The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex. Nat Struct Biol. 1995, 2: 386-394.CrossRefPubMed
12.
Zurück zum Zitat Brzozowski AM, Pike AC, Dauter Z, Hubbard RE, Bonn T, Engstrom O, Ohman L, Greene GL, Gustafsson JA, Carlquist M: Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 1997, 389: 753-758. 10.1038/39645., This study presents the first structure of an antagonist-bound NR LBD, and compares at the molecular level the distinct conformation of estradiol- or raloxifene-bound LBDsCrossRefPubMed Brzozowski AM, Pike AC, Dauter Z, Hubbard RE, Bonn T, Engstrom O, Ohman L, Greene GL, Gustafsson JA, Carlquist M: Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 1997, 389: 753-758. 10.1038/39645., This study presents the first structure of an antagonist-bound NR LBD, and compares at the molecular level the distinct conformation of estradiol- or raloxifene-bound LBDsCrossRefPubMed
13.
Zurück zum Zitat Tanenbaum DM, Wang Y, Williams SP, Sigler PB: Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci USA. 1998, 95: 5998-6003. 10.1073/pnas.95.11.5998.CrossRefPubMedPubMedCentral Tanenbaum DM, Wang Y, Williams SP, Sigler PB: Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci USA. 1998, 95: 5998-6003. 10.1073/pnas.95.11.5998.CrossRefPubMedPubMedCentral
14.
Zurück zum Zitat 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. 1995, 375: 377-382. 10.1038/375377a0., This study presents the first structure of an apolipoprotein NR LBD, and defines the canonical fold for members of the NR familyCrossRefPubMed 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. 1995, 375: 377-382. 10.1038/375377a0., This study presents the first structure of an apolipoprotein NR LBD, and defines the canonical fold for members of the NR familyCrossRefPubMed
15.
Zurück zum Zitat Danielian PS, White R, Lees JA, Parker MG: Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors [published erratum appears in EMBO J 1992, 11:2366]. EMBO J. 1992, 11: 1025-1033.PubMedPubMedCentral Danielian PS, White R, Lees JA, Parker MG: Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors [published erratum appears in EMBO J 1992, 11:2366]. EMBO J. 1992, 11: 1025-1033.PubMedPubMedCentral
16.
Zurück zum Zitat Moras D, Gronemeyer H: The nuclear receptor ligand-binding domain: structure and function. Curr Opin Cell Biol. 1998, 10: 384-391. 10.1016/S0955-0674(98)80015-X., This study reviews the structural basis for the specific recognition of ligands and provides a comprehensive view of the early steps of nuclear receptor actionCrossRefPubMed Moras D, Gronemeyer H: The nuclear receptor ligand-binding domain: structure and function. Curr Opin Cell Biol. 1998, 10: 384-391. 10.1016/S0955-0674(98)80015-X., This study reviews the structural basis for the specific recognition of ligands and provides a comprehensive view of the early steps of nuclear receptor actionCrossRefPubMed
17.
Zurück zum Zitat Kumar V, Chambon P: The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell. 1988, 55: 145-156.CrossRefPubMed Kumar V, Chambon P: The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell. 1988, 55: 145-156.CrossRefPubMed
18.
Zurück zum Zitat Fawell SE, White R, Hoare S, Sydenham M, Page M, Parker MG: Inhibition of estrogen receptor-DNA binding by the 'pure' antiestrogen ICI 164,384 appears to be mediated by impaired receptor dimerization. Proc Natl Acad Sci USA. 1990, 87: 6883-6887.CrossRefPubMedPubMedCentral Fawell SE, White R, Hoare S, Sydenham M, Page M, Parker MG: Inhibition of estrogen receptor-DNA binding by the 'pure' antiestrogen ICI 164,384 appears to be mediated by impaired receptor dimerization. Proc Natl Acad Sci USA. 1990, 87: 6883-6887.CrossRefPubMedPubMedCentral
19.
Zurück zum Zitat Pike AC, Brzozowski AM, Hubbard RE, Bonn T, Thorsell AG, Engstrom O, Ljunggren J, Gustafsson JA, Carlquist M: Structure of the ligand-binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist. EMBO J. 1999, 18: 4608-4618. 10.1093/emboj/18.17.4608., This comparison of the ERa and ERb LBDs shows a suboptimal alignment of the transactivation helix, which is consistent with genistein’s partial agonist character in ERb and demonstrates how the transcriptional response of ER to certain bound ligands is modulatedCrossRefPubMedPubMedCentral Pike AC, Brzozowski AM, Hubbard RE, Bonn T, Thorsell AG, Engstrom O, Ljunggren J, Gustafsson JA, Carlquist M: Structure of the ligand-binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist. EMBO J. 1999, 18: 4608-4618. 10.1093/emboj/18.17.4608., This comparison of the ERa and ERb LBDs shows a suboptimal alignment of the transactivation helix, which is consistent with genistein’s partial agonist character in ERb and demonstrates how the transcriptional response of ER to certain bound ligands is modulatedCrossRefPubMedPubMedCentral
20.
Zurück zum Zitat Williams SP, Sigler PB: Atomic structure of progesterone complexed with its receptor. Nature. 1998, 393: 392-396. 10.1038/30775., This study describes a different mode of dimerization for PR LBD, compared with ER and RXRCrossRefPubMed Williams SP, Sigler PB: Atomic structure of progesterone complexed with its receptor. Nature. 1998, 393: 392-396. 10.1038/30775., This study describes a different mode of dimerization for PR LBD, compared with ER and RXRCrossRefPubMed
21.
Zurück zum Zitat Xu J, Nawaz Z, Tsai SY, Tsai MJ, O'Malley BW: The extreme C terminus of the progesterone receptor contains a transcriptional repressor domain that functions through a putative corepressor. Proc Natl Acad Sci USA. 1996, 93: 12195-12199. 10.1073/pnas.93.22.12195.CrossRefPubMedPubMedCentral Xu J, Nawaz Z, Tsai SY, Tsai MJ, O'Malley BW: The extreme C terminus of the progesterone receptor contains a transcriptional repressor domain that functions through a putative corepressor. Proc Natl Acad Sci USA. 1996, 93: 12195-12199. 10.1073/pnas.93.22.12195.CrossRefPubMedPubMedCentral
22.
Zurück zum Zitat Zhang S, Liang X, Danielsen M: Role of the C terminus of the glucocorticoid receptor in hormone binding and agonist/antagonist discrimination. Mol Endocrinol. 1996, 10: 24-34. 10.1210/me.10.1.24.PubMed Zhang S, Liang X, Danielsen M: Role of the C terminus of the glucocorticoid receptor in hormone binding and agonist/antagonist discrimination. Mol Endocrinol. 1996, 10: 24-34. 10.1210/me.10.1.24.PubMed
23.
Zurück zum Zitat Lanz RB, Rusconi S: A conserved carboxy-terminal subdomain is important for ligand interpretation and transactivation by nuclear receptors. Endocrinology. 1994, 135: 2183-2195. 10.1210/en.135.5.2183.PubMed Lanz RB, Rusconi S: A conserved carboxy-terminal subdomain is important for ligand interpretation and transactivation by nuclear receptors. Endocrinology. 1994, 135: 2183-2195. 10.1210/en.135.5.2183.PubMed
24.
Zurück zum Zitat Jenster G, van der Korput HA, van Vroonhoven C, van der Kwast TH, Trapman J, Brinkmann AO: Domains of the human androgen receptor involved in steroid binding, transcriptional activation, and sub-cellular localization. Mol Endocrinol. 1991, 5: 1396-1404.CrossRefPubMed Jenster G, van der Korput HA, van Vroonhoven C, van der Kwast TH, Trapman J, Brinkmann AO: Domains of the human androgen receptor involved in steroid binding, transcriptional activation, and sub-cellular localization. Mol Endocrinol. 1991, 5: 1396-1404.CrossRefPubMed
25.
Zurück zum Zitat Ogawa S, Inoue S, Watanabe T, Orimo A, Hosoi T, Ouchi Y, Muramatsu M: Molecular cloning and characterization of human estrogen receptor betacx: a potential inhibitor ofestrogen action in human. Nucleic Acids Res. 1998, 26: 3505-3512. 10.1093/nar/26.15.3505.CrossRefPubMedPubMedCentral Ogawa S, Inoue S, Watanabe T, Orimo A, Hosoi T, Ouchi Y, Muramatsu M: Molecular cloning and characterization of human estrogen receptor betacx: a potential inhibitor ofestrogen action in human. Nucleic Acids Res. 1998, 26: 3505-3512. 10.1093/nar/26.15.3505.CrossRefPubMedPubMedCentral
26.
Zurück zum Zitat Renaud JP, 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. 1995, 378: 681-689. 10.1038/378681a0., This study proposes a ‘mouse trap’ mechanism whereby a ligand-induced conformational transition repositions the amphipathic alpha-helix of the AF-2 activating domain and forms a transcriptionally active receptorCrossRefPubMed Renaud JP, 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. 1995, 378: 681-689. 10.1038/378681a0., This study proposes a ‘mouse trap’ mechanism whereby a ligand-induced conformational transition repositions the amphipathic alpha-helix of the AF-2 activating domain and forms a transcriptionally active receptorCrossRefPubMed
27.
Zurück zum Zitat Wurtz JM, Bourguet W, Renaud JP, Vivat V, Chambon P, Moras D, Gronemeyer H: A canonical structure for the ligand-binding domain of nuclear receptors [published erratum appears in Nat Struct Biol 1996, 3:206]. Nat Struct Biol. 1996, 3: 87-94.CrossRefPubMed Wurtz JM, Bourguet W, Renaud JP, Vivat V, Chambon P, Moras D, Gronemeyer H: A canonical structure for the ligand-binding domain of nuclear receptors [published erratum appears in Nat Struct Biol 1996, 3:206]. Nat Struct Biol. 1996, 3: 87-94.CrossRefPubMed
28.
Zurück zum Zitat Darimont BD, Wagner RL, Apriletti JW, Stallcup MR, Kushner PJ, Baxter JD, Fletterick RJ, Yamamoto KR: Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev. 1998, 12: 3343-3356.CrossRefPubMedPubMedCentral Darimont BD, Wagner RL, Apriletti JW, Stallcup MR, Kushner PJ, Baxter JD, Fletterick RJ, Yamamoto KR: Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev. 1998, 12: 3343-3356.CrossRefPubMedPubMedCentral
29.
Zurück zum Zitat Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV: Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 1998, 395: 137-143. 10.1038/25931., This study describes the ternary complex containing the peroxysome proliferator activated receptor-gamma LBD, the antidiabetic ligand rosiglitazone, and 88 amino acids of human SRC-1, and suggests a general mechanism for the assembly of nuclear receptors with coactivatorsCrossRefPubMed Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV: Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 1998, 395: 137-143. 10.1038/25931., This study describes the ternary complex containing the peroxysome proliferator activated receptor-gamma LBD, the antidiabetic ligand rosiglitazone, and 88 amino acids of human SRC-1, and suggests a general mechanism for the assembly of nuclear receptors with coactivatorsCrossRefPubMed
30.
Zurück zum Zitat Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, Agard DA, Greene GL: The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell. 1998, 95: 927-937. 10.1016/S0092-8674(00)81717-1., This study presents crystal structures of human ERa LBD bound to both the agonist DES and a peptide derived from the NR box II region of the coactivator TIF2/GRIP1, and bound to the selective antagonist 4-hydroxytamoxifen, revealing the two distinct mechanisms by which structural features of 4-hydroxytamoxifen promote the ‘autoinhibitory’ helix-12 conformationCrossRefPubMed Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, Agard DA, Greene GL: The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell. 1998, 95: 927-937. 10.1016/S0092-8674(00)81717-1., This study presents crystal structures of human ERa LBD bound to both the agonist DES and a peptide derived from the NR box II region of the coactivator TIF2/GRIP1, and bound to the selective antagonist 4-hydroxytamoxifen, revealing the two distinct mechanisms by which structural features of 4-hydroxytamoxifen promote the ‘autoinhibitory’ helix-12 conformationCrossRefPubMed
31.
Zurück zum Zitat Anstead GM, Carlson KE, Katzenellenbogen JA: The estradiol pharmacophore: ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site. Steroids. 1997, 62: 268-303. 10.1016/S0039-128X(96)00242-5.CrossRefPubMed Anstead GM, Carlson KE, Katzenellenbogen JA: The estradiol pharmacophore: ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site. Steroids. 1997, 62: 268-303. 10.1016/S0039-128X(96)00242-5.CrossRefPubMed
32.
Zurück zum Zitat Grese TA, Pennington LD, Sluka JP, Adrian MD, Cole HW, Fuson TR, Magee DE, Phillips DL, Rowley ER, Shetler PK, Short LL, Venugopalan M, Yang NN, Sato M, Glasebrook AL, Bryant HU: Synthesis and pharmacology of conformationally restricted raloxifene analogues: highly potent selective estrogen receptor modulators. J Med Chem. 1998, 41: 1272-1283. 10.1021/jm970688z.CrossRefPubMed Grese TA, Pennington LD, Sluka JP, Adrian MD, Cole HW, Fuson TR, Magee DE, Phillips DL, Rowley ER, Shetler PK, Short LL, Venugopalan M, Yang NN, Sato M, Glasebrook AL, Bryant HU: Synthesis and pharmacology of conformationally restricted raloxifene analogues: highly potent selective estrogen receptor modulators. J Med Chem. 1998, 41: 1272-1283. 10.1021/jm970688z.CrossRefPubMed
33.
Zurück zum Zitat Kuiper GG, Lemmen JG, Carlsson B, Corton JC, Safe SH, van der Saag PT, van der Burg B, Gustafsson JA: Interaction of estrogenic chemicals and phytoestrogens with estrogen receptor beta. Endocrinology. 1998, 139: 4252-4263. 10.1210/en.139.10.4252.PubMed Kuiper GG, Lemmen JG, Carlsson B, Corton JC, Safe SH, van der Saag PT, van der Burg B, Gustafsson JA: Interaction of estrogenic chemicals and phytoestrogens with estrogen receptor beta. Endocrinology. 1998, 139: 4252-4263. 10.1210/en.139.10.4252.PubMed
Metadaten
Titel
Estrogen receptor transcription and transactivation Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors
verfasst von
Marc Ruff
Monique Gangloff
Jean Marie Wurtz
Dino Moras
Publikationsdatum
01.10.2000
Verlag
BioMed Central
Erschienen in
Breast Cancer Research / Ausgabe 5/2000
Elektronische ISSN: 1465-542X
DOI
https://doi.org/10.1186/bcr80

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