메뉴 건너뛰기




Volumn 15, Issue 4, 2006, Pages 722-730

Conformational changes of the glucocorticoid receptor ligand binding domain induced by ligand and cofactor binding, and the location of cofactor binding sites determined by hydrogen/deuterium exchange mass spectrometry

Author keywords

Glucocorticoid receptor; H D exchange; Mass spectrometry

Indexed keywords

DEXAMETHASONE; GLUCOCORTICOID RECEPTOR; MIFEPRISTONE; NUCLEAR RECEPTOR COACTIVATOR 2; NUCLEAR RECEPTOR COREPRESSOR;

EID: 33645512016     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051781406     Document Type: Article
Times cited : (41)

References (23)
  • 1
    • 0033773479 scopus 로고    scopus 로고
    • Molecular mechanisms of glucocorticoid actions
    • Adcock, I.M. 2000. Molecular mechanisms of glucocorticoid actions. Pulm. Pharmacol. Ther. 13: 115-126.
    • (2000) Pulm. Pharmacol. Ther. , vol.13 , pp. 115-126
    • Adcock, I.M.1
  • 2
    • 18444405534 scopus 로고    scopus 로고
    • Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition
    • Bledsoe, R.K., Montana, V.G., Stanley, T.B., Delves, C.J., Apolito, C.J., McKee, D.D., Consler, T.G., Parks, D.J., Stewart, E.L., Willson, T.M., et al. 2002. Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell 110: 93-105.
    • (2002) Cell , vol.110 , pp. 93-105
    • Bledsoe, R.K.1    Montana, V.G.2    Stanley, T.B.3    Delves, C.J.4    Apolito, C.J.5    McKee, D.D.6    Consler, T.G.7    Parks, D.J.8    Stewart, E.L.9    Willson, T.M.10
  • 3
    • 0032600473 scopus 로고    scopus 로고
    • Determining affinity-selected ligands and estimating binding affinities by online size exclusion chromatography/liquid chromatography-mass spectrometry
    • Blom, K.F., Larsen, B.S., and McEwen, C.N. 1999. Determining affinity-selected ligands and estimating binding affinities by online size exclusion chromatography/liquid chromatography-mass spectrometry. J. Comb. Chem. 1: 82-90.
    • (1999) J. Comb. Chem. , vol.1 , pp. 82-90
    • Blom, K.F.1    Larsen, B.S.2    McEwen, C.N.3
  • 7
    • 0034636021 scopus 로고    scopus 로고
    • Glucocorticoids repress NF-κB-driven genes by disturbing the interaction of p65 with the basal transcription machinery, irrespective of coactivator levels in the cell
    • De Bosscher, K., Vanden Berghe,W., Vermeulen, L., Plaisance, S., Boone, E., and Haegeman, G. 2000. Glucocorticoids repress NF-κB-driven genes by disturbing the interaction of p65 with the basal transcription machinery, irrespective of coactivator levels in the cell. Proc. Natl. Acad. Sci. 97: 3919-3924.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 3919-3924
    • De Bosscher, K.1    Vanden Berghe, W.2    Vermeulen, L.3    Plaisance, S.4    Boone, E.5    Haegeman, G.6
  • 8
    • 0033551496 scopus 로고    scopus 로고
    • Hydrogen exchange shows peptide binding stabilizes motions in Hck SH2
    • Engen, J.R., Gmeiner, W.H., Smithgall, T.E., and Smith, D.L. 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
  • 9
    • 9644307891 scopus 로고    scopus 로고
    • Glucocorticoid ligands specify different interactions with NF-κB by allosteric effects on the glucocorticoid receptor DNA binding domain
    • Garside, H., Stevens, A., Farrow, S., Normand, C., Hould, B., Berry, A., Maschera, B., and Ray, D. 2004. Glucocorticoid ligands specify different interactions with NF-κB by allosteric effects on the glucocorticoid receptor DNA binding domain. J. Biol. Chem. 48: 50050-50059.
    • (2004) J. Biol. Chem. , vol.48 , pp. 50050-50059
    • Garside, H.1    Stevens, A.2    Farrow, S.3    Normand, C.4    Hould, B.5    Berry, A.6    Maschera, B.7    Ray, D.8
  • 10
    • 0023649643 scopus 로고
    • Cooperativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene
    • Jantzen, H.-M., Strahle, U., Gloss, B., Stewart, F., Schmid, W., Boshart, M., Miksicek, R., and Schutz, G. 1987. Cooperativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene. Cell 49: 29-38.
    • (1987) Cell , vol.49 , pp. 29-38
    • Jantzen, H.-M.1    Strahle, U.2    Gloss, B.3    Stewart, F.4    Schmid, W.5    Boshart, M.6    Miksicek, R.7    Schutz, G.8
  • 13
    • 77956736670 scopus 로고    scopus 로고
    • New insights into glucocorticoid and mineralocorticoid signaling: Lessons from gene targeting
    • Reichardt, H.M., Tronche, F., Berger, S., Kellendonk, C., and Schutz, G. 2000. New insights into glucocorticoid and mineralocorticoid signaling: Lessons from gene targeting. Adv. Pharmacol. 47: 1-21.
    • (2000) Adv. Pharmacol. , vol.47 , pp. 1-21
    • Reichardt, H.M.1    Tronche, F.2    Berger, S.3    Kellendonk, C.4    Schutz, G.5
  • 14
    • 0032512423 scopus 로고    scopus 로고
    • Deuterium exchange mass spectrometry as a probe of protein kinase activation. Analysis of wild type and constitutively active mutants of MAP kinase kinase-1
    • Resing, K.A. and Ahn, N.G. 1998. Deuterium exchange mass spectrometry as a probe of protein kinase activation. Analysis of wild type and constitutively active mutants of MAP kinase kinase-1. Biochemistry 37: 463-475.
    • (1998) Biochemistry , vol.37 , pp. 463-475
    • Resing, K.A.1    Ahn, N.G.2
  • 15
    • 0033474495 scopus 로고    scopus 로고
    • Modeling deuterium exchange behavior of ERK2 using peptide mapping to probe secondary structure
    • Resing, K.A., Hoofnagle, A.N., and Ahn, N.G. 1999. Modeling deuterium exchange behavior of ERK2 using peptide mapping to probe secondary structure. J. Am. Soc. Mass Spectrom. 10: 685-702.
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 685-702
    • Resing, K.A.1    Hoofnagle, A.N.2    Ahn, N.G.3
  • 17
    • 0036810356 scopus 로고    scopus 로고
    • Mechanisms involved in the side effects of glucocorticoids
    • Schacke, H., Docke, W.-D., and Asadullah, K. 2002. Mechanisms involved in the side effects of glucocorticoids. Pharmacol. Ther. 96: 23-43.
    • (2002) Pharmacol. Ther. , vol.96 , pp. 23-43
    • Schacke, H.1    Docke, W.-D.2    Asadullah, K.3
  • 18
    • 0347719371 scopus 로고    scopus 로고
    • Dissociation of transactivation from transrepression by a selective glucorticoid receptor agonist leads to separation of therapeutic effects from side effects
    • Schacke, H., Schottelius, A., Docke, W., Strehlke, P., Jaroch, S., Schmees, N., Rehwinkel, H., Hennekes, H., and Asadullah, K. 2004. Dissociation of transactivation from transrepression by a selective glucorticoid receptor agonist leads to separation of therapeutic effects from side effects. Proc. Natl. Acad. Sci. 101: 227-232.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 227-232
    • Schacke, H.1    Schottelius, A.2    Docke, W.3    Strehlke, P.4    Jaroch, S.5    Schmees, N.6    Rehwinkel, H.7    Hennekes, H.8    Asadullah, K.9
  • 19
    • 0037135577 scopus 로고    scopus 로고
    • RU486-induced glucocorticoid receptor agonism is controlled by the receptor N terminus and by corepressor binding
    • Schulz, M., Eggert, M., Baniahmad, A., Dostert, A., Heinzel, T., and Renkawitz, R. 2002. RU486-induced glucocorticoid receptor agonism is controlled by the receptor N terminus and by corepressor binding. J. Biol. Chem. 277: 26238-26243.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26238-26243
    • Schulz, M.1    Eggert, M.2    Baniahmad, A.3    Dostert, A.4    Heinzel, T.5    Renkawitz, R.6
  • 20
    • 0033428390 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometric detection of small Ca (2+)-induced conformational changes in the regulatory domain of human cardiac troponin c
    • Wang, F., Li, W., Emmett, M.R., Marshall, A.G., Corson, D., and Sykes, B.D. 1999. Fourier transform ion cyclotron resonance mass spectrometric detection of small Ca (2+)-induced conformational changes in the regulatory domain of human cardiac troponin c. J. Am. Soc. Mass Spectrom. 10: 703-710.
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 703-710
    • Wang, F.1    Li, W.2    Emmett, M.R.3    Marshall, A.G.4    Corson, D.5    Sykes, B.D.6
  • 21
    • 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, M.E., Schimerlik, M.I., and Deinzer, M.L. 2004. 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.
    • (2004) Biochemistry , vol.43 , pp. 909-917
    • Yan, X.1    Broderick, D.2    Leid, M.E.3    Schimerlik, M.I.4    Deinzer, M.L.5
  • 22
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang, Z.Q. and Smith, D.L. 1993. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci. 2: 522-531.
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.Q.1    Smith, D.L.2
  • 23
    • 0030046197 scopus 로고    scopus 로고
    • Amide hydrogen exchange determined by mass spectrometry: Application to rabbit muscle aldolase
    • Zhang, Z.Q., Post, C.B., and Smith, D.L. 1996. Amide hydrogen exchange determined by mass spectrometry: Application to rabbit muscle aldolase. Biochemistry 35: 779-791.
    • (1996) Biochemistry , vol.35 , pp. 779-791
    • Zhang, Z.Q.1    Post, C.B.2    Smith, D.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.