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Volumn 25, Issue 1, 2011, Pages 15-31

Analysis of agonist and antagonist effects on thyroid hormone receptor conformation by hydrogen/deuterium exchange

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; AMMONIA; BINDING PROTEIN; DEUTERIUM; DIMER; HORMONE RECEPTOR AFFECTING AGENT; HORMONE RECEPTOR BLOCKING AGENT; HYDROGEN; LIGAND; LIGAND BINDING PROTEIN; PEPTIDE; SOLVENT; THYROID HORMONE RECEPTOR; THYROID HORMONE RECEPTOR AGONIST; THYROID HORMONE RECEPTOR ANTAGONIST; UNCLASSIFIED DRUG;

EID: 78650854003     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2010-0202     Document Type: Article
Times cited : (40)

References (66)
  • 2
    • 0034650893 scopus 로고    scopus 로고
    • The corregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG 2000 The corregulator 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
  • 3
    • 0025687882 scopus 로고
    • Nuclear thyroid receptor
    • Lazar MA, Chin WW 1990 Nuclear thyroid receptor. J Clin Invest 86: 1777-1782
    • (1990) J Clin Invest , vol.86 , pp. 1777-1782
    • Lazar, M.A.1    Chin, W.W.2
  • 7
    • 3242784885 scopus 로고    scopus 로고
    • Mechanism of the nuclear receptor molecular switch
    • Nagy L, Schwabe JWR 2004 Mechanism of the nuclear receptor molecular switch. Trends Biochem Sci 29: 317-324
    • (2004) Trends Biochem Sci , vol.29 , pp. 317-324
    • Nagy, L.1    Schwabe, J.W.R.2
  • 11
    • 18044365802 scopus 로고    scopus 로고
    • Conformational adaptation of nuclear receptor ligand binding domains to agonists: Potential for novel approaches to ligand design
    • Togashi M, Borngraeber S, Sandler B, Fletterick RJ, Webb P, Baxter JD 2005 Conformational adaptation of nuclear receptor ligand binding domains to agonists: Potential for novel approaches to ligand design. J Steroid Biochem Mol Biol 93: 127-137
    • (2005) J Steroid Biochem Mol Biol , vol.93 , pp. 127-137
    • Togashi, M.1    Borngraeber, S.2    Sandler, B.3    Fletterick, R.J.4    Webb, P.5    Baxter, J.D.6
  • 12
    • 0035805580 scopus 로고    scopus 로고
    • Definition of the surface in the thyroid hormone receptor ligand binding domain for association as homodimers and heterodimers with retinoid X receptor
    • Ribeiro RC, Feng W, Wagner RL, Costa CH, Pereira AC, Apriletti JW, Fletterick RJ, Baxter JD 2001 Definition of the surface in the thyroid hormone receptor ligand binding domain for association as homodimers and heterodimers with retinoid X receptor. J Biol Chem 276: 14987-14995
    • (2001) J Biol Chem , vol.276 , pp. 14987-14995
    • Ribeiro, R.C.1    Feng, W.2    Wagner, R.L.3    Costa, C.H.4    Pereira, A.C.5    Apriletti, J.W.6    Fletterick, R.J.7    Baxter, J.D.8
  • 16
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-R
    • Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D 1995 Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-R. 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
  • 17
    • 34249847751 scopus 로고    scopus 로고
    • Structural insights into corepressor recognition by antagonist-bound estrogen receptors
    • Heldring N, Pawson T, McDonnell D, Treuter E, Gustafsson JA, Pike AC 2007 Structural insights into corepressor recognition by antagonist-bound estrogen receptors. J Biol Chem 282: 10449-10455
    • (2007) J Biol Chem , vol.282 , pp. 10449-10455
    • Heldring, N.1    Pawson, T.2    McDonnell, D.3    Treuter, E.4    Gustafsson, J.A.5    Pike, A.C.6
  • 19
    • 0032906662 scopus 로고    scopus 로고
    • Unbinding of retinoic acid from its receptor studied by steered molecular dynamics
    • Kosztin D, Izrailev S, Schulten K 1999 Unbinding of retinoic acid from its receptor studied by steered molecular dynamics. Biophys J 76: 188-197
    • (1999) Biophys J , vol.76 , pp. 188-197
    • Kosztin, D.1    Izrailev, S.2    Schulten, K.3
  • 20
    • 0034724560 scopus 로고    scopus 로고
    • Ligand-induced stabilization of PPAR-γ monitored by NMR spectroscopy: Implications for nuclear receptor activation
    • Johnson BA, Wilson EM, Li Y, Moller DE, Smith RG, ZhouG2000 Ligand-induced stabilization of PPAR-γ monitored by NMR spectroscopy: Implications for nuclear receptor activation. J Mol Biol 298: 187-194
    • (2000) J Mol Biol , vol.298 , pp. 187-194
    • Johnson, B.A.1    Wilson, E.M.2    Li, Y.3    Moller, D.E.4    Smith, R.G.5    Zhou, G.6
  • 22
    • 33645512016 scopus 로고    scopus 로고
    • Conformational changes of the glucocorticoid receptor ligand binding domain induced by ligand and cofactor binding, and the location of cofactor binding sites deter- mined by hydrogen/deuterium exchange mass spectrometry
    • Frego L, Davidson W 2006 Conformational changes of the glucocorticoid receptor ligand binding domain induced by ligand and cofactor binding, and the location of cofactor binding sites deter- mined by hydrogen/deuterium exchange mass spectrometry. Protein Sci 15: 722-730
    • (2006) Protein Sci , vol.15 , pp. 722-730
    • Frego, L.1    Davidson, W.2
  • 23
    • 0942290634 scopus 로고    scopus 로고
    • Dynamics and ligand-induced solvent accessibility changes in human retinoid X receptor homodimer determined by hydrogen deuterium exchange and mass spectrometry
    • Yan X, Broderick D, Leid ME, Schimerlik MI, Deinzer ML 2003 Dynamics and ligand-induced solvent accessibility changes in human retinoid X receptor homodimer determined by hydrogen deuterium exchange and mass spectrometry. Biochemistry 43: 909-917
    • (2003) Biochemistry , vol.43 , pp. 909-917
    • Yan, X.1    Broderick, D.2    Leid, M.E.3    Schimerlik, M.I.4    Deinzer, M.L.5
  • 24
    • 0033637850 scopus 로고    scopus 로고
    • Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding
    • Pissios P, Tzameli I, Kushner P, Moore DD 2000 Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding. Mol Cell 6: 245-253
    • (2000) Mol Cell , vol.6 , pp. 245-253
    • Pissios, P.1    Tzameli, I.2    Kushner, P.3    Moore, D.D.4
  • 26
    • 0037249279 scopus 로고    scopus 로고
    • Thyroid hormone receptor-β mutations conferring hormone resistance and reduced corepressor release exhibit decreased stability in the N-terminal ligand-binding domain
    • Huber BR, Desclozeaux M, West BL, Cunha-Lima ST, Nguyen HT, Baxter JD, Ingraham HA, Fletterick RJ 2003 Thyroid hormone receptor-β mutations conferring hormone resistance and reduced corepressor release exhibit decreased stability in the N-terminal ligand-binding domain. Mol Endocrinol 17: 107-116
    • (2003) Mol Endocrinol , vol.17 , pp. 107-116
    • Huber, B.R.1    Desclozeaux, M.2    West, B.L.3    Cunha-Lima, S.T.4    Nguyen, H.T.5    Baxter, J.D.6    Ingraham, H.A.7    Fletterick, R.J.8
  • 29
    • 0033551496 scopus 로고    scopus 로고
    • Hydrogen exchange shows peptide binding stabilizes motions in Hck SH2
    • Engen JR, Gmeiner WH, Smithgall TE, Smith DL 1999 Hydrogen exchange shows peptide binding stabilizes motions in Hck SH2. Biochemistry 38: 8926-8935
    • (1999) Biochemistry , vol.38 , pp. 8926-8935
    • Engen, J.R.1    Gmeiner, W.H.2    Smithgall, T.E.3    Smith, D.L.4
  • 33
    • 35648986229 scopus 로고    scopus 로고
    • Deuterium exchange and mass spectrometry reveal the interaction differences of two synthetic modulators of RXR LBD
    • Yan X, Pérez E, Leid M, Schimerlik MI, de Lera AR, Deinzer ML 2007 Deuterium exchange and mass spectrometry reveal the interaction differences of two synthetic modulators of RXR LBD. Protein Sci 16: 2491-2501
    • (2007) Protein Sci , vol.16 , pp. 2491-2501
    • Yan, X.1    Pérez, E.2    Leid, M.3    Schimerlik, M.I.4    De Lera, A.R.5    Deinzer, M.L.6
  • 35
    • 33644751845 scopus 로고    scopus 로고
    • Impaired helix 12 dynamics due to proline 892 substitutions in the androgen receptor are associated with complete androgen insensitivity
    • Elhaji YA, Stoica I, Dennis S, Purisima EO, Lumbroso R, Beitel LK, Trifiro MA 2006 Impaired helix 12 dynamics due to proline 892 substitutions in the androgen receptor are associated with complete androgen insensitivity. Hum Mol Genet 15: 921-931
    • (2006) Hum Mol Genet , vol.15 , pp. 921-931
    • Elhaji, Y.A.1    Stoica, I.2    Dennis, S.3    Purisima, E.O.4    Lumbroso, R.5    Beitel, L.K.6    Trifiro, M.A.7
  • 36
    • 46149089650 scopus 로고    scopus 로고
    • Preliminary molecular dynamic simulations of estrogen receptor-β ligand binding domain from antagonist to apo
    • McGee TD, Edwards J, Roitberg AE 2008 Preliminary molecular dynamic simulations of estrogen receptor-β ligand binding domain from antagonist to apo. Int J Environ Res Public Health 5: 111-114
    • (2008) Int J Environ Res Public Health , vol.5 , pp. 111-114
    • McGee, T.D.1    Edwards, J.2    Roitberg, A.E.3
  • 37
    • 33847114057 scopus 로고    scopus 로고
    • Conformational dynamics of the estrogen receptor-β: Molecular dynamics simulations of the influence of binding site structure on protein dynamics
    • Celik L, Lund JD, Schiøtt B 2007 Conformational dynamics of the estrogen receptor-β: Molecular dynamics simulations of the influence of binding site structure on protein dynamics. Biochemistry 46: 1743-1758
    • (2007) Biochemistry , vol.46 , pp. 1743-1758
    • Celik, L.1    Lund, J.D.2    Schiøtt, B.3
  • 38
    • 46349088224 scopus 로고    scopus 로고
    • Ligand dissociation from estrogen receptor is mediated by receptor dimerization: Evidence from molecular dynamics simulations
    • Sonoda MT, Martínez L, Webb P, Skaf MS, Polikarpov I 2008 Ligand dissociation from estrogen receptor is mediated by receptor dimerization: Evidence from molecular dynamics simulations. Mol Endocrinol 22: 1565-1578
    • (2008) Mol Endocrinol , vol.22 , pp. 1565-1578
    • Sonoda, M.T.1    Martínez, L.2    Webb, P.3    Skaf, M.S.4    Polikarpov, I.5
  • 39
    • 30444446327 scopus 로고    scopus 로고
    • Molecular Dynamics simulations of ligand dissociation from thyroid hormone receptors: Evidence of the likeliest escape pathway and its implications for the design of novel ligands
    • Martínez L, Webb P, Polikarpov I, Skaf MS 2006 Molecular Dynamics simulations of ligand dissociation from thyroid hormone receptors: Evidence of the likeliest escape pathway and its implications for the design of novel ligands. J Med Chem 49: 23-26
    • (2006) J Med Chem , vol.49 , pp. 23-26
    • Martínez, L.1    Webb, P.2    Polikarpov, I.3    Skaf, M.S.4
  • 40
    • 24144439756 scopus 로고    scopus 로고
    • Molecular dynamics simulations reveal multiple pathways of ligand dissociation from thyroid hormone receptors
    • Martínez L, Sonoda MT, Webb P, Baxter JD, Skaf MS, Polikarpov I 2005 Molecular dynamics simulations reveal multiple pathways of ligand dissociation from thyroid hormone receptors. Biophys J 89: 2011-2023
    • (2005) Biophys J , vol.89 , pp. 2011-2023
    • Martínez, L.1    Sonoda, M.T.2    Webb, P.3    Baxter, J.D.4    Skaf, M.S.5    Polikarpov, I.6
  • 43
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, Agard DA, Greene GL 1998 The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95: 927-937
    • (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
  • 44
    • 0032807750 scopus 로고    scopus 로고
    • A novel role for helix 12 of retinoid X receptor in regulating repression
    • Zhang J, Hu X, LazarMA1999 A novel role for helix 12 of retinoid X receptor in regulating repression. Mol Cell Biol 19: 6448-6457
    • (1999) Mol Cell Biol , vol.19 , pp. 6448-6457
    • Zhang, J.1    Hu, X.2    Lazar, M.A.3
  • 46
    • 21844450222 scopus 로고    scopus 로고
    • Rearrangements in thyroid hormone receptor charge clusters that stabilize bound 3,5',5-triiodo-L-thyronine and inhibit homodimer formation
    • Togashi M, Nguyen P, Fletterick R, Baxter JD, Webb P 2005 Rearrangements in thyroid hormone receptor charge clusters that stabilize bound 3,5',5-triiodo-L-thyronine and inhibit homodimer formation. J Biol Chem 280: 25665-25673
    • (2005) J Biol Chem , vol.280 , pp. 25665-25673
    • Togashi, M.1    Nguyen, P.2    Fletterick, R.3    Baxter, J.D.4    Webb, P.5
  • 50
    • 0037130243 scopus 로고    scopus 로고
    • Rational design and synthesis of a novel thyroid hormone antagonist that blocks coactivator recruitment
    • Nguyen NH, Apriletti JW, Cunha Lima ST, Webb P, Baxter JD, Scanlan TS 2002 Rational design and synthesis of a novel thyroid hormone antagonist that blocks coactivator recruitment. J Med Chem 45: 3310-3320
    • (2002) J Med Chem , vol.45 , pp. 3310-3320
    • Nguyen, N.H.1    Apriletti, J.W.2    Cunha Lima, S.T.3    Webb, P.4    Baxter, J.D.5    Scanlan, T.S.6
  • 52
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser KM, Baker P, Burlingame AL 1999 Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal Chem 71: 2871-2882
    • (1999) Anal Chem , vol.71 , pp. 2871-2882
    • Clauser, K.M.1    Baker, P.2    Burlingame, A.L.3
  • 53
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C 1983 Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 54
    • 0033625531 scopus 로고    scopus 로고
    • TeXshade: Shading and labeling of multiple sequence alignments using LaTeX2e
    • Beitz E 2000 TeXshade: Shading and labeling of multiple sequence alignments using LaTeX2e. Bioinformatics 16: 135-139
    • (2000) Bioinformatics , vol.16 , pp. 135-139
    • Beitz, E.1
  • 55
    • 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 JD, Higgins DG, Gibson TJ 1994 CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 56
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL 1993 Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 234: 779-815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 60
    • 17944391445 scopus 로고    scopus 로고
    • Packing optimization for automated generation of complex system's initial configurations for molecular dynamics and docking
    • Martínez JM, Martínez L 2003 Packing optimization for automated generation of complex system's initial configurations for molecular dynamics and docking. J Comput Chem 24: 819-825
    • (2003) J Comput Chem , vol.24 , pp. 819-825
    • Martínez, J.M.1    Martínez, L.2
  • 61
    • 69949118458 scopus 로고    scopus 로고
    • A package for building initial configurations for molecular dynamics simulations
    • Martínez L, Andrade R, Birgin EG, Martínez JM 2009 A package for building initial configurations for molecular dynamics simulations. J Comput Chem 30: 2157-2164
    • (2009) J Comput Chem , vol.30 , pp. 2157-2164
    • Martínez, L.1    Andrade, R.2    Birgin, E.G.3    Martínez, J.M.4
  • 65
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An Nlog(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L 1993 Particle mesh Ewald: An Nlog(N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 66
    • 0002404088 scopus 로고
    • On the orthogonal transformation used for structural comparisons
    • Kearsley SK 1989 On the orthogonal transformation used for structural comparisons. Acta Cryst A 45: 208-210
    • (1989) Acta Cryst A , vol.45 , pp. 208-210
    • Kearsley, S.K.1


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