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Volumn 17, Issue 7, 2003, Pages 1283-1295

Crystal structure and nuclear magnetic resonance analyses of the SAND domain from glucocorticoid modulatory element binding protein-1 reveals deoxyribonucleic acid and zinc binding regions

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; DNA; GLUCOCORTICOID MODULATORY ELEMENT BINDING PROTEIN 1; GLUCOCORTICOID MODULATORY ELEMENT BINDING PROTEIN 2; PROTEIN; PROTEIN AIRE1; PROTEIN DEAF1; PROTEIN NUCP41 75; PROTEIN SP100; STEROID HORMONE; UNCLASSIFIED DRUG; ZINC;

EID: 0038309923     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2002-0409     Document Type: Article
Times cited : (40)

References (54)
  • 1
    • 0026658867 scopus 로고
    • Higher levels of control: Modulation of steroid hormone-regulated gene transcription
    • Simons Jr SS, Oshima H, Szapary D 1992 Higher levels of control: modulation of steroid hormone-regulated gene transcription. Mol Endocrinol 6:995-1002
    • (1992) Mol Endocrinol , vol.6 , pp. 995-1002
    • Simons S.S., Jr.1    Oshima, H.2    Szapary, D.3
  • 2
    • 0034712937 scopus 로고    scopus 로고
    • Ability of the glucocorticoid modulatory element to modify glucocorticoid receptor transactivation indicates parallel pathways for the expression of glucocorticoid modulatory element and glucocorticoid response element activities
    • Zeng H, Plisov SY, Simons Jr SS 2000 Ability of the glucocorticoid modulatory element to modify glucocorticoid receptor transactivation indicates parallel pathways for the expression of glucocorticoid modulatory element and glucocorticoid response element activities. Mol Cell Endocrinol 162:221-234
    • (2000) Mol Cell Endocrinol , vol.162 , pp. 221-234
    • Zeng, H.1    Plisov, S.Y.2    Simons S.S., Jr.3
  • 3
    • 0027772883 scopus 로고
    • Sequence-selective interactions of transcription factor elements with tandem glucocorticoid-responsive elements at physiological steroid concentrations
    • Oshima H, Simons Jr SS 1993 Sequence-selective interactions of transcription factor elements with tandem glucocorticoid-responsive elements at physiological steroid concentrations. J Biol Chem 268:26858-26865
    • (1993) J Biol Chem , vol.268 , pp. 26858-26865
    • Oshima, H.1    Simons S.S., Jr.2
  • 4
    • 0026514404 scopus 로고
    • Modulation of transcription factor activity by a distant steroid modulatory element
    • Oshima H, Simons Jr SS 1992 Modulation of transcription factor activity by a distant steroid modulatory element. Mol Endocrinol 6:416-428
    • (1992) Mol Endocrinol , vol.6 , pp. 416-428
    • Oshima, H.1    Simons S.S., Jr.2
  • 5
    • 0029974456 scopus 로고    scopus 로고
    • A negative tyrosine aminotransferase gene element that blocks glucocorticoid modulatory element-regulated modulation of glucocorticoid-induced gene expression
    • Collier CD, Oshima H, Simons Jr SS 1996 A negative tyrosine aminotransferase gene element that blocks glucocorticoid modulatory element-regulated modulation of glucocorticoid-induced gene expression. Mol Endocrinol 10:463-476
    • (1996) Mol Endocrinol , vol.10 , pp. 463-476
    • Collier, C.D.1    Oshima, H.2    Simons S.S., Jr.3
  • 7
    • 0037077274 scopus 로고    scopus 로고
    • Structure/activity elements of the multifunctional protein, GMEB-1. Characterization of domains relevant for the modulation of glucocorticoid receptor transactivation properties
    • Chen J, Kaul S, Simons Jr SS 2002 Structure/activity elements of the multifunctional protein, GMEB-1. Characterization of domains relevant for the modulation of glucocorticoid receptor transactivation properties. J Biol Chem 277:22053-22062
    • (2002) J Biol Chem , vol.277 , pp. 22053-22062
    • Chen, J.1    Kaul, S.2    Simons S.S., Jr.3
  • 8
    • 0033974844 scopus 로고    scopus 로고
    • Cloning of a mouse glucocorticoid modulatory element binding protein, a new member of the KDWK family
    • Jimenez-Lara AM, Heine MJ, Gronemeyer H 2000 Cloning of a mouse glucocorticoid modulatory element binding protein, a new member of the KDWK family. FEBS Lett 468:203-210
    • (2000) FEBS Lett , vol.468 , pp. 203-210
    • Jimenez-Lara, A.M.1    Heine, M.J.2    Gronemeyer, H.3
  • 9
    • 0029097635 scopus 로고
    • The factor binding to the glucocorticoid modulatory element of the tyrosine aminotransferase gene is a novel and ubiquitous heteromeric complex
    • Oshima H, Szapary D, Simons Jr SS 1995 The factor binding to the glucocorticoid modulatory element of the tyrosine aminotransferase gene is a novel and ubiquitous heteromeric complex. J Biol Chem 270:21893-21901
    • (1995) J Biol Chem , vol.270 , pp. 21893-21901
    • Oshima, H.1    Szapary, D.2    Simons S.S., Jr.3
  • 10
    • 0344417221 scopus 로고    scopus 로고
    • Cloning and characterization of hGMEB1, a novel glucocorticoid modulatory element binding protein
    • Theriault JR, Charette SJ, Lambert H, Landry J 1999 Cloning and characterization of hGMEB1, a novel glucocorticoid modulatory element binding protein. FEBS Lett 452:170-176
    • (1999) FEBS Lett , vol.452 , pp. 170-176
    • Theriault, J.R.1    Charette, S.J.2    Lambert, H.3    Landry, J.4
  • 11
    • 0032504201 scopus 로고    scopus 로고
    • Cloning and characterization of a novel binding factor (GMEB-2) of the glucocorticoid modulatory element
    • Zeng H, Jackson DA, Oshima H, Simons Jr SS 1998 Cloning and characterization of a novel binding factor (GMEB-2) of the glucocorticoid modulatory element. J Biol Chem 273:17756-17762
    • (1998) J Biol Chem , vol.273 , pp. 17756-17762
    • Zeng, H.1    Jackson, D.A.2    Oshima, H.3    Simons S.S., Jr.4
  • 12
    • 0034463535 scopus 로고    scopus 로고
    • Properties of the glucocorticoid modulatory element binding proteins GMEB-1 and -2: Potential new modifiers of glucocorticoid receptor transactivation and members of the family of KDWK proteins
    • Kaul S, Blackford Jr JA, Chen J, Ogryzko W, Simons Jr SS 2000 Properties of the glucocorticoid modulatory element binding proteins GMEB-1 and -2: potential new modifiers of glucocorticoid receptor transactivation and members of the family of KDWK proteins. Mol Endocrinol 14:1010-1027
    • (2000) Mol Endocrinol , vol.14 , pp. 1010-1027
    • Kaul, S.1    Blackford J.A., Jr.2    Chen, J.3    Ogryzko, W.4    Simons S.S., Jr.5
  • 13
    • 0030738386 scopus 로고    scopus 로고
    • Parvovirus initiation factor PIF: A novel human DNA-binding factor which coordinately recognizes two ACGT motifs
    • Christensen J, Cotmore SF, Tattersall P 1997 Parvovirus initiation factor PIF: a novel human DNA-binding factor which coordinately recognizes two ACGT motifs. J Virol 71:5733-5741
    • (1997) J Virol , vol.71 , pp. 5733-5741
    • Christensen, J.1    Cotmore, S.F.2    Tattersall, P.3
  • 14
    • 0031031923 scopus 로고    scopus 로고
    • A novel cellular site-specific DNA-binding protein cooperates with the viral NS1 polypeptide to initiate parvovirus DNA replication
    • Christensen J, Cotmore SF, Tattersall P 1997 A novel cellular site-specific DNA-binding protein cooperates with the viral NS1 polypeptide to initiate parvovirus DNA replication. J Virol 71:1405-1416
    • (1997) J Virol , vol.71 , pp. 1405-1416
    • Christensen, J.1    Cotmore, S.F.2    Tattersall, P.3
  • 15
    • 0032722209 scopus 로고    scopus 로고
    • Two new members of the emerging KDWK family of combinatorial transcription modulators bind as a heterodimer to flexibly spaced PuCGPy half-sites
    • Christensen J, Cotmore SF, Tattersall P 1999 Two new members of the emerging KDWK family of combinatorial transcription modulators bind as a heterodimer to flexibly spaced PuCGPy half-sites. Mol Cell Biol 19:7741-7750
    • (1999) Mol Cell Biol , vol.19 , pp. 7741-7750
    • Christensen, J.1    Cotmore, S.F.2    Tattersall, P.3
  • 16
    • 0032127876 scopus 로고    scopus 로고
    • The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor
    • Gibson TJ, Ramu C, Gemund C, Aasland R 1998 The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor. Trends Biochem Sci 23:242-244
    • (1998) Trends Biochem Sci , vol.23 , pp. 242-244
    • Gibson, T.J.1    Ramu, C.2    Gemund, C.3    Aasland, R.4
  • 17
    • 0033860185 scopus 로고    scopus 로고
    • Sp110 localizes to the PML-Sp100 nuclear body and may function as a nuclear hormone receptor transcriptional coactivator
    • Bloch DB, Nakajima A, Gulick T, Chiche JD, Orth D, de La Monte SM, Bloch KD 2000 Sp110 localizes to the PML-Sp100 nuclear body and may function as a nuclear hormone receptor transcriptional coactivator. Mol Cell Biol 20:6138-6146
    • (2000) Mol Cell Biol , vol.20 , pp. 6138-6146
    • Bloch, D.B.1    Nakajima, A.2    Gulick, T.3    Chiche, J.D.4    Orth, D.5    De La Monte, S.M.6    Bloch, K.D.7
  • 18
    • 0029831827 scopus 로고    scopus 로고
    • Identification and characterization of a leukocyte-specific component of the nuclear body
    • Bloch DB, de la Monte SM, Guigaouri P, Filippov A, Bloch KD 1996 Identification and characterization of a leukocyte-specific component of the nuclear body. J Biol Chem 271:29198-29204
    • (1996) J Biol Chem , vol.271 , pp. 29198-29204
    • Bloch, D.B.1    De La Monte, S.M.2    Guigaouri, P.3    Filippov, A.4    Bloch, K.D.5
  • 20
    • 0029986957 scopus 로고    scopus 로고
    • DEAF-1, a novel protein that binds an essential region in a deformed response element
    • Gross CT, McGinnis W 1996 DEAF-1, a novel protein that binds an essential region in a deformed response element. EMBO J 15:1961-1970
    • (1996) EMBO J , vol.15 , pp. 1961-1970
    • Gross, C.T.1    McGinnis, W.2
  • 21
    • 0032230281 scopus 로고    scopus 로고
    • Characterization of a nuclear deformed epidermal autoregulatory factor-1 (DEAF-1)-related (NUDR) transcriptional regulator protein
    • Huggenvik JI, Michelson RJ, Collard MW, Ziemba AJ, Gurley P, Mowen KA 1998 Characterization of a nuclear deformed epidermal autoregulatory factor-1 (DEAF-1)-related (NUDR) transcriptional regulator protein. Mol Endocrinol 12:1619-1639
    • (1998) Mol Endocrinol , vol.12 , pp. 1619-1639
    • Huggenvik, J.I.1    Michelson, R.J.2    Collard, M.W.3    Ziemba, A.J.4    Gurley, P.5    Mowen, K.A.6
  • 22
    • 0036079307 scopus 로고    scopus 로고
    • DEAF-1 function is essential for the early embryonic development of Drosophila
    • Veraksa A, Kennison J, McGinnis W 2002 DEAF-1 function is essential for the early embryonic development of Drosophila. Genesis 33:67-76
    • (2002) Genesis , vol.33 , pp. 67-76
    • Veraksa, A.1    Kennison, J.2    McGinnis, W.3
  • 24
    • 0032725046 scopus 로고    scopus 로고
    • Nuclear DEAF-1-related (NUDR) protein contains a novel DNA binding domain and represses transcription of the heterogeneous nuclear ribonucleoprotein A2/B1 promoter
    • Michelson RJ, Collard MW, Ziemba AJ, Persinger J, Bartholomew B, Huggenvik JI 1999 Nuclear DEAF-1-related (NUDR) protein contains a novel DNA binding domain and represses transcription of the heterogeneous nuclear ribonucleoprotein A2/B1 promoter. J Biol Chem 274:30510-30519
    • (1999) J Biol Chem , vol.274 , pp. 30510-30519
    • Michelson, R.J.1    Collard, M.W.2    Ziemba, A.J.3    Persinger, J.4    Bartholomew, B.5    Huggenvik, J.I.6
  • 26
    • 0037790522 scopus 로고    scopus 로고
    • Autoimmune regulator: From loss of function to autoimmunity
    • Pitkanen J, Peterson P 2003 Autoimmune regulator: from loss of function to autoimmunity. Genes Immun 4:12-21
    • (2003) Genes Immun , vol.4 , pp. 12-21
    • Pitkanen, J.1    Peterson, P.2
  • 27
    • 0032231606 scopus 로고    scopus 로고
    • Structure, organization, and dynamics of promyelocytic leukemia protein nuclear bodies
    • Hodges M, Tissot C, Howe K, Grimwade D, Freemont PS 1998 Structure, organization, and dynamics of promyelocytic leukemia protein nuclear bodies. Am J Hum Genet 63:297-304
    • (1998) Am J Hum Genet , vol.63 , pp. 297-304
    • Hodges, M.1    Tissot, C.2    Howe, K.3    Grimwade, D.4    Freemont, P.S.5
  • 28
    • 0032560469 scopus 로고    scopus 로고
    • Chromatin components as part of a putative transcriptional repressing complex
    • Lehming N, Le Saux A, Schuller J, Ptashne M 1998 Chromatin components as part of a putative transcriptional repressing complex. Proc Natl Acad Sci USA 95:7322-7326
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7322-7326
    • Lehming, N.1    Le Saux, A.2    Schuller, J.3    Ptashne, M.4
  • 29
    • 0032560477 scopus 로고    scopus 로고
    • Interaction of SP100 with HP1 proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment
    • Seeler JS, Marchio A, Sitterlin D, Transy C, Dejean A 1998 Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc Natl Acad Sci USA 95: 7316-7321
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7316-7321
    • Seeler, J.S.1    Marchio, A.2    Sitterlin, D.3    Transy, C.4    Dejean, A.5
  • 30
    • 0036848069 scopus 로고    scopus 로고
    • Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: Insights on Ski-mediated repression of TGF-β signaling
    • Wu JW, Krawitz AR, Chai J, Li W, Zhang F, Luo K, Shi Y 2002 Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-β signaling. Cell 111:357-367
    • (2002) Cell , vol.111 , pp. 357-367
    • Wu, J.W.1    Krawitz, A.R.2    Chai, J.3    Li, W.4    Zhang, F.5    Luo, K.6    Shi, Y.7
  • 32
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • Alberts IL, Nadassy K, Wodak SJ 1998 Analysis of zinc binding sites in protein crystal structures. Protein Sci 7:1700-1716
    • (1998) Protein Sci , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 33
    • 0035253128 scopus 로고    scopus 로고
    • Retinoid X receptor and its partners in the nuclear receptor family
    • Rastinejad F 2001 Retinoid X receptor and its partners in the nuclear receptor family. Curr Opin Struct Biol 11:33-38
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 33-38
    • Rastinejad, F.1
  • 34
    • 0027222793 scopus 로고
    • Structure of the retinoid X receptor α DNA binding domain: A helix required for homodimeric DNA binding
    • Lee MS, Kliewer SA, Provencal J, Wright PE, Evans RM 1993 Structure of the retinoid X receptor α DNA binding domain: a helix required for homodimeric DNA binding. Science 260:1117-1121
    • (1993) Science , vol.260 , pp. 1117-1121
    • Lee, M.S.1    Kliewer, S.A.2    Provencal, J.3    Wright, P.E.4    Evans, R.M.5
  • 36
    • 0036020490 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Coding a diversity of proteins and responses through a single gene
    • Yudt MR, Cidlowski JA 2002 The glucocorticoid receptor: coding a diversity of proteins and responses through a single gene. Mol Endocrinol 16:1719-1726
    • (2002) Mol Endocrinol , vol.16 , pp. 1719-1726
    • Yudt, M.R.1    Cidlowski, J.A.2
  • 41
    • 0035861985 scopus 로고    scopus 로고
    • A consensus DNA recognition motif for two KDWK transcription factors identifies flexible-length, CpG-methylation sensitive cognate binding sites in the majority of human promoters
    • Burnett E, Christensen J, Tattersall P 2001 A consensus DNA recognition motif for two KDWK transcription factors identifies flexible-length, CpG-methylation sensitive cognate binding sites in the majority of human promoters. J Mol Biol 314:1029-1039
    • (2001) J Mol Biol , vol.314 , pp. 1029-1039
    • Burnett, E.1    Christensen, J.2    Tattersall, P.3
  • 43
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W 1993 Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26:795-800
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 45
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M 1991 Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 46
    • 0027787894 scopus 로고
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J Am Chem Soc 115:12593-12594
    • (1993) J Am Chem Soc , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 47
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M, Schleucher J, Griesinger C 1999 Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog NMR Spectrosc 34:93-158
    • (1999) Prog NMR Spectrosc , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 49
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson B, Blevins RA 1994 NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4:603-614
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.1    Blevins, R.A.2
  • 50
    • 0031933143 scopus 로고    scopus 로고
    • Determining the structures of large proteins and protein complexes by NMR
    • Clore GM, Gronenborn AM 1998 Determining the structures of large proteins and protein complexes by NMR. Trends Biotechnol 16:22-34
    • (1998) Trends Biotechnol , vol.16 , pp. 22-34
    • Clore, G.M.1    Gronenborn, A.M.2
  • 51
    • 0037354262 scopus 로고    scopus 로고
    • 1H, 13C and 15N backbone resonance assignments of the SAND domains from the glucocorticoid modulatory element binding proteins-1 and -2
    • Bottomley MJ, Sattler M 2003 1H, 13C and 15N backbone resonance assignments of the SAND domains from the glucocorticoid modulatory element binding proteins-1 and -2. J Biomol NMR 25:259-260
    • (2003) J Biomol NMR , vol.25 , pp. 259-260
    • Bottomley, M.J.1    Sattler, M.2
  • 52
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K 1996 MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14:51-55
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 53
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG 1997 The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 54
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B 1991 Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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