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Volumn 113, Issue 3-5, 2009, Pages 253-258

Structural changes of vitamin D receptor induced by 20-epi-1α,25-(OH)2D3: An insight from a computational analysis

Author keywords

20 epi Vitamin D analogs; Structure comparisons; Targets for mutational analyses; Vitamin D; Vitamin D receptor

Indexed keywords

20 EPICALCITRIOL; CALCITRIOL; NUCLEAR RECEPTOR COACTIVATOR 2; RETINOID X RECEPTOR; STEROID RECEPTOR COACTIVATOR 1; VITAMIN D RECEPTOR;

EID: 61349112664     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2009.01.007     Document Type: Article
Times cited : (9)

References (39)
  • 2
    • 0033963897 scopus 로고    scopus 로고
    • The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand
    • Rochel N., Wurtz J.M., Mitschler A., Klaholz B., and Moras D. The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand. Mol. Cell 5 (2000) 173-179
    • (2000) Mol. Cell , vol.5 , pp. 173-179
    • Rochel, N.1    Wurtz, J.M.2    Mitschler, A.3    Klaholz, B.4    Moras, D.5
  • 4
    • 33947109474 scopus 로고    scopus 로고
    • Adaptability of the vitamin D nuclear receptor to the synthetic ligand Gemini: remodeling the LBP with one side chain rotation
    • Ciesielski F., Rochel N., and Moras D. Adaptability of the vitamin D nuclear receptor to the synthetic ligand Gemini: remodeling the LBP with one side chain rotation. J. Steroid. Biochem. Mol. Biol. 103 (2007) 235-242
    • (2007) J. Steroid. Biochem. Mol. Biol. , vol.103 , pp. 235-242
    • Ciesielski, F.1    Rochel, N.2    Moras, D.3
  • 6
    • 33746380300 scopus 로고    scopus 로고
    • Ligand binding domain of vitamin D receptors
    • Rochel N., and Moras D. Ligand binding domain of vitamin D receptors. Curr. Top. Med. Chem. 6 (2006) 1229-1241
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 1229-1241
    • Rochel, N.1    Moras, D.2
  • 8
    • 61349094920 scopus 로고    scopus 로고
    • H.F. DeLuca, J. Wicha, 20(S)-25-hydroxy vitamin D compounds, US Patent 5,840,938, 1998
    • H.F. DeLuca, J. Wicha, 20(S)-25-hydroxy vitamin D compounds, US Patent 5,840,938. (1998).
  • 10
    • 0037217046 scopus 로고    scopus 로고
    • Structure-function relationships of vitamin D including ligand recognition by the vitamin D receptor
    • Yamada S., Shimizu M., and Yamamoto K. Structure-function relationships of vitamin D including ligand recognition by the vitamin D receptor. Med. Res. Rev. 23 (2003) 89-115
    • (2003) Med. Res. Rev. , vol.23 , pp. 89-115
    • Yamada, S.1    Shimizu, M.2    Yamamoto, K.3
  • 12
    • 33947127037 scopus 로고    scopus 로고
    • Computational analysis of the active sites in binary and ternary complexes of the vitamin D receptor
    • Conference Communicate on 13th Workshop on Vitamin D, Special Issue
    • Sicinska W., and Rotkiewicz P. Computational analysis of the active sites in binary and ternary complexes of the vitamin D receptor. Conference Communicate on 13th Workshop on Vitamin D, Special Issue. J. Steroid Biochem. Mol. Biol. 103 (2007) 305-309
    • (2007) J. Steroid Biochem. Mol. Biol. , vol.103 , pp. 305-309
    • Sicinska, W.1    Rotkiewicz, P.2
  • 14
    • 61349203037 scopus 로고    scopus 로고
    • CCOMP version 3.30
    • CCOMP version 3.30, http://www.pirx.com/ccomp
  • 17
    • 33746274738 scopus 로고    scopus 로고
    • DFT calculation of nitrogen chemical shifts in the active site of vitamin D receptor
    • Sicinska W. DFT calculation of nitrogen chemical shifts in the active site of vitamin D receptor. Polish J. Chem. 80 (2006) 1177-1183
    • (2006) Polish J. Chem. , vol.80 , pp. 1177-1183
    • Sicinska, W.1
  • 18
    • 27544439435 scopus 로고    scopus 로고
    • NMR assignments of tryptophan residue in apo and holo LBD-rVDR
    • Sicinska W., Westler W.M., and DeLuca H.F. NMR assignments of tryptophan residue in apo and holo LBD-rVDR. Proteins 61 (2005) 461-467
    • (2005) Proteins , vol.61 , pp. 461-467
    • Sicinska, W.1    Westler, W.M.2    DeLuca, H.F.3
  • 19
    • 0036667731 scopus 로고    scopus 로고
    • Rotamer libraries in the 21st century
    • Dunbrack R.L. Rotamer libraries in the 21st century. Curr. Opin. Struct. Biol. 12 (2002) 431-440
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 431-440
    • Dunbrack, R.L.1
  • 20
    • 0033582329 scopus 로고    scopus 로고
    • Asparagine and glutamine rotamers: B-factor cutoff and correction of amide flips yield distinct clustering
    • Lovell S.C., Word J.M., Richardson J.S., and Richardson D.C. Asparagine and glutamine rotamers: B-factor cutoff and correction of amide flips yield distinct clustering. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 400-405
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 400-405
    • Lovell, S.C.1    Word, J.M.2    Richardson, J.S.3    Richardson, D.C.4
  • 24
    • 0032802247 scopus 로고    scopus 로고
    • 3 and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties
    • 3 and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties. Mol. Cell. Biol. 19 (1999) 5486-5494
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5486-5494
    • Lavigne, A.C.1    Mengus, G.2    Gangloff, Y.G.3    Wurtz, J.M.4    Davidson, I.5
  • 25
    • 0036784897 scopus 로고    scopus 로고
    • Structurally and functionally important amino acids of the agonistic conformation of the human vitamin D receptor
    • Vaisanen S., Ryhanen S., Saarela J.T.A., Perakyla M., Andersin T., and Maenpaa P.H. Structurally and functionally important amino acids of the agonistic conformation of the human vitamin D receptor. Mol. Pharmacol. 62 (2002) 788-794
    • (2002) Mol. Pharmacol. , vol.62 , pp. 788-794
    • Vaisanen, S.1    Ryhanen, S.2    Saarela, J.T.A.3    Perakyla, M.4    Andersin, T.5    Maenpaa, P.H.6
  • 26
    • 9244262737 scopus 로고    scopus 로고
    • A unique insertion/substitution in helix H1 of the vitamin D receptor ligand binding domain in a patient with hereditary 1,25-dihydroxyvitamin D-resistant rickets
    • Malloy P.J., Xu R., Cattani A., Reyes L., and Feldman D. A unique insertion/substitution in helix H1 of the vitamin D receptor ligand binding domain in a patient with hereditary 1,25-dihydroxyvitamin D-resistant rickets. J. Bone Miner. Res. 19 (2004) 1018-1024
    • (2004) J. Bone Miner. Res. , vol.19 , pp. 1018-1024
    • Malloy, P.J.1    Xu, R.2    Cattani, A.3    Reyes, L.4    Feldman, D.5
  • 27
    • 61349152564 scopus 로고    scopus 로고
    • http://www.usm.maine.edu/∼rhodes/SPVTut/text/STut09aTN.html.
  • 29
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • Chothia C. The nature of the accessible and buried surfaces in proteins. J. Mol. Biol. 105 (1976) 1-14
    • (1976) J. Mol. Biol. , vol.105 , pp. 1-14
    • Chothia, C.1
  • 30
    • 61349159452 scopus 로고    scopus 로고
    • SYBYL Modeling Program, 7.1 ed., Tripos Inc., St. Louis, MO, 2005.
    • SYBYL Modeling Program, 7.1 ed., Tripos Inc., St. Louis, MO, 2005.
  • 34
    • 0037424534 scopus 로고    scopus 로고
    • Interactions of SKIP/NCoA-62, TFIIB and retinoid X receptor with vitamin D receptor helix H10 residues
    • Barry J.B., Leong G.M., Church W.B., Issa L.L., Eisman J.A., and Gardiner E.M. Interactions of SKIP/NCoA-62, TFIIB and retinoid X receptor with vitamin D receptor helix H10 residues. J. Biol. Chem. 278 (2003) 8224-8228
    • (2003) J. Biol. Chem. , vol.278 , pp. 8224-8228
    • Barry, J.B.1    Leong, G.M.2    Church, W.B.3    Issa, L.L.4    Eisman, J.A.5    Gardiner, E.M.6
  • 36
    • 3042713982 scopus 로고    scopus 로고
    • Emerging insights into the coactivator role of NCoA62/SKIP in vitamin D-mediated transcription
    • MacDonald P.N., Dowd D.R., Zhang C., and Gu C. Emerging insights into the coactivator role of NCoA62/SKIP in vitamin D-mediated transcription. J. Steroid. Biochem. Mol. Biol. 89-90 (2004) 179-186
    • (2004) J. Steroid. Biochem. Mol. Biol. , vol.89-90 , pp. 179-186
    • MacDonald, P.N.1    Dowd, D.R.2    Zhang, C.3    Gu, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.