메뉴 건너뛰기




Volumn 15, Issue 4, 2008, Pages 383-392

Structure-Based Design of a Superagonist Ligand for the Vitamin D Nuclear Receptor

Author keywords

CHEMBIO; SIGNALING

Indexed keywords

CALCITRIOL; CALCITRIOL RECEPTOR; DRUG DERIVATIVE; LIGAND; VITAMIN D;

EID: 41949120325     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2008.03.016     Document Type: Article
Times cited : (56)

References (45)
  • 1
    • 0142181197 scopus 로고    scopus 로고
    • Antiproliferative role of vitamin D and its analogs-a brief overview
    • Banerjee P., and Chatterjee M. Antiproliferative role of vitamin D and its analogs-a brief overview. Mol. Cell. Biochem. 253 (2003) 247-254
    • (2003) Mol. Cell. Biochem. , vol.253 , pp. 247-254
    • Banerjee, P.1    Chatterjee, M.2
  • 4
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet W., Ruff M., Chambon P., Gronemeyer H., and Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 375 (1995) 377-382
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 6
    • 33749252164 scopus 로고    scopus 로고
    • The vitamin D receptor as a therapeutic target
    • Campbell M.J., and Adorini L. The vitamin D receptor as a therapeutic target. Expert Opin. Ther. Targets 10 (2006) 735-748
    • (2006) Expert Opin. Ther. Targets , vol.10 , pp. 735-748
    • Campbell, M.J.1    Adorini, L.2
  • 7
    • 33746618050 scopus 로고    scopus 로고
    • The impact of chromatin organization of vitamin D target genes
    • Carlberg C., and Dunlop T.W. The impact of chromatin organization of vitamin D target genes. Anticancer Res. 26 (2006) 2637-2645
    • (2006) Anticancer Res. , vol.26 , pp. 2637-2645
    • Carlberg, C.1    Dunlop, T.W.2
  • 8
    • 10944248801 scopus 로고    scopus 로고
    • Mouse functional genomics requires standardization of mouse handling and housing conditions
    • Champy M.F., Selloum M., Piard L., Zeitler V., Caradec C., Chambon P., and Auwerx J. Mouse functional genomics requires standardization of mouse handling and housing conditions. Mamm. Genome 15 (2004) 768-783
    • (2004) Mamm. Genome , vol.15 , pp. 768-783
    • Champy, M.F.1    Selloum, M.2    Piard, L.3    Zeitler, V.4    Caradec, C.5    Chambon, P.6    Auwerx, J.7
  • 10
    • 33947109474 scopus 로고    scopus 로고
    • Adaptability of the vitamin D nuclear receptor to the synthetic ligand Gemini: remodelling 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: remodelling 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
  • 11
    • 33644895955 scopus 로고    scopus 로고
    • Vitamin D signaling is modulated on multiple levels in health and disease
    • Ebert R., Schütze N., Adamski J., and Jakob F. Vitamin D signaling is modulated on multiple levels in health and disease. Mol. Cell. Endocrinol. 248 (2006) 149-159
    • (2006) Mol. Cell. Endocrinol. , vol.248 , pp. 149-159
    • Ebert, R.1    Schütze, N.2    Adamski, J.3    Jakob, F.4
  • 13
    • 0034669784 scopus 로고    scopus 로고
    • Aldose and aldehyde reductases: correlation of molecular modeling and mass spectrometric studies on the binding of inhibitors to the active site
    • El-Kabbani O., Rogniaux H., Barth P., Chung R.P.-T., Fletcher E.V., Van Dorsselear A., and Podjarny A. Aldose and aldehyde reductases: correlation of molecular modeling and mass spectrometric studies on the binding of inhibitors to the active site. Proteins 41 (2000) 407-414
    • (2000) Proteins , vol.41 , pp. 407-414
    • El-Kabbani, O.1    Rogniaux, H.2    Barth, P.3    Chung, R.P.-T.4    Fletcher, E.V.5    Van Dorsselear, A.6    Podjarny, A.7
  • 15
    • 8044226035 scopus 로고    scopus 로고
    • Combination of a potent 20-epi-vitamin D3 analogue (KH1060) with 9-cis-retinoic acid irreversibly inhibits clonal growth, decreases bcl-2 expression, and induces apoptosis in HL-60 leukemic cells
    • Elstner E., Linker-Israeli M., Umiel T., Le J., Grillier I., Said J., Shintaku I.P., Krajewski S., Reed J.C., Binderup L., et al. Combination of a potent 20-epi-vitamin D3 analogue (KH1060) with 9-cis-retinoic acid irreversibly inhibits clonal growth, decreases bcl-2 expression, and induces apoptosis in HL-60 leukemic cells. Cancer Res. 56 (1996) 3570-3576
    • (1996) Cancer Res. , vol.56 , pp. 3570-3576
    • Elstner, E.1    Linker-Israeli, M.2    Umiel, T.3    Le, J.4    Grillier, I.5    Said, J.6    Shintaku, I.P.7    Krajewski, S.8    Reed, J.C.9    Binderup, L.10
  • 17
    • 0037302906 scopus 로고    scopus 로고
    • Vitamin D: a millenium perspective
    • Holick M.F. Vitamin D: a millenium perspective. J. Cell. Biochem. 88 (2003) 296-307
    • (2003) J. Cell. Biochem. , vol.88 , pp. 296-307
    • Holick, M.F.1
  • 18
    • 33747452055 scopus 로고    scopus 로고
    • Probing a water channel near the A-ring of receptor-bound 1α,25-dihydroxyvitamin D3 with selected 2α-substituted analogues
    • Hourai S., Fujishima T., Kittaka A., Suhara Y., Takayama H., Rochel N., and Moras D. Probing a water channel near the A-ring of receptor-bound 1α,25-dihydroxyvitamin D3 with selected 2α-substituted analogues. J. Med. Chem. 49 (2006) 5199-5205
    • (2006) J. Med. Chem. , vol.49 , pp. 5199-5205
    • Hourai, S.1    Fujishima, T.2    Kittaka, A.3    Suhara, Y.4    Takayama, H.5    Rochel, N.6    Moras, D.7
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 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
  • 20
    • 0035175877 scopus 로고    scopus 로고
    • The practical synthesis of vitamin D analogs: a challenge for process research
    • Kabat M.M., and Radinov R. The practical synthesis of vitamin D analogs: a challenge for process research. Curr. Opin. Drug Discov. Devel. 4 (2001) 808-833
    • (2001) Curr. Opin. Drug Discov. Devel. , vol.4 , pp. 808-833
    • Kabat, M.M.1    Radinov, R.2
  • 22
    • 33646133406 scopus 로고    scopus 로고
    • The expanding cosmos of nuclear receptor coactivators
    • Lonard D.M., and O'Malley B.W. The expanding cosmos of nuclear receptor coactivators. Cell 125 (2006) 411-414
    • (2006) Cell , vol.125 , pp. 411-414
    • Lonard, D.M.1    O'Malley, B.W.2
  • 23
    • 37049095544 scopus 로고
    • Synthetic approaches to vitamin D and its relatives
    • Lythgoe B. Synthetic approaches to vitamin D and its relatives. Chem. Soc. Rev. 9 (1980) 449-475
    • (1980) Chem. Soc. Rev. , vol.9 , pp. 449-475
    • Lythgoe, B.1
  • 24
    • 0020577903 scopus 로고
    • 1,25-dihydroxyvitamin D3 inhibits proliferation of human promyelocytic leukaemia (HL60) cells and induces monocyte-macrophage differentiation in HL60 and normal human bone marrow cells
    • McCarthy D.M., San Miguel J.F., Freake H.C., Green P.M., Zola H., Catovsky D., and Goldman J.M. 1,25-dihydroxyvitamin D3 inhibits proliferation of human promyelocytic leukaemia (HL60) cells and induces monocyte-macrophage differentiation in HL60 and normal human bone marrow cells. Leuk. Res. 7 (1983) 51-55
    • (1983) Leuk. Res. , vol.7 , pp. 51-55
    • McCarthy, D.M.1    San Miguel, J.F.2    Freake, H.C.3    Green, P.M.4    Zola, H.5    Catovsky, D.6    Goldman, J.M.7
  • 26
    • 23744437421 scopus 로고    scopus 로고
    • Noncalcemic actions of vitamin D receptors ligands
    • Nagpal S., Na S., and Rathnachalam R. Noncalcemic actions of vitamin D receptors ligands. Endocr. Rev. 26 (2005) 662-687
    • (2005) Endocr. Rev. , vol.26 , pp. 662-687
    • Nagpal, S.1    Na, S.2    Rathnachalam, R.3
  • 27
    • 0345874610 scopus 로고    scopus 로고
    • Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model
    • Norman A.W., Mizwicki M.T., and Norman D.P. Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model. Nat. Rev. Drug Discov. 3 (2004) 27-41
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 27-41
    • Norman, A.W.1    Mizwicki, M.T.2    Norman, D.P.3
  • 28
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate S.A., Tsai S.Y., Tsai M.J., and O'Malley B.W. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270 (1995) 1354-1357
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.J.3    O'Malley, B.W.4
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0028980556 scopus 로고
    • Vitamin D3 analogs: effect on leukemic clonal growth and differentiation, and on serum calcium levels
    • Pakkala S., de Vos S., Elstner E., Rude R.K., Uskokovic M., Binderup L., and Koeffler H.P. Vitamin D3 analogs: effect on leukemic clonal growth and differentiation, and on serum calcium levels. Leuk. Res. 19 (1995) 65-72
    • (1995) Leuk. Res. , vol.19 , pp. 65-72
    • Pakkala, S.1    de Vos, S.2    Elstner, E.3    Rude, R.K.4    Uskokovic, M.5    Binderup, L.6    Koeffler, H.P.7
  • 31
    • 0028917557 scopus 로고
    • Distinct conformational changes induced by 20-epi analogues of 1α,25-dihydroxyvitamin D3 are associated with enhanced activation of the vitamin D receptor
    • Peleg S., Sastry M., Collins E.D., Bishop J.E., and Norman A.W. Distinct conformational changes induced by 20-epi analogues of 1α,25-dihydroxyvitamin D3 are associated with enhanced activation of the vitamin D receptor. J. Biol. Chem. 270 (1995) 10551-10558
    • (1995) J. Biol. Chem. , vol.270 , pp. 10551-10558
    • Peleg, S.1    Sastry, M.2    Collins, E.D.3    Bishop, J.E.4    Norman, A.W.5
  • 34
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
    • Renaud J.P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., and Moras D. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378 (1995) 681-689
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.P.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 35
    • 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
  • 36
    • 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
  • 37
    • 0035064150 scopus 로고    scopus 로고
    • Functional and structural characterization of the insertion region in the ligand binding domain of the vitamin D nuclear receptor
    • Rochel N., Tocchini-Valentini G., Egea P.F., Juntunen K., Garnier J.M., Vihko P., and Moras D. Functional and structural characterization of the insertion region in the ligand binding domain of the vitamin D nuclear receptor. Eur. J. Biochem. 268 (2001) 971-979
    • (2001) Eur. J. Biochem. , vol.268 , pp. 971-979
    • Rochel, N.1    Tocchini-Valentini, G.2    Egea, P.F.3    Juntunen, K.4    Garnier, J.M.5    Vihko, P.6    Moras, D.7
  • 40
    • 1842607351 scopus 로고    scopus 로고
    • Crystal structures of the vitamin D nuclear receptor liganded with the vitamin D side chain analogues calcipotriol and seocalcitol, receptor agonists of clinical importance. Insights into a structural basis for the switching of calcipotriol to a receptor antagonist by further side chain modification
    • Tocchini-Valentini G., Rochel N., Wurtz J.M., and Moras D. Crystal structures of the vitamin D nuclear receptor liganded with the vitamin D side chain analogues calcipotriol and seocalcitol, receptor agonists of clinical importance. Insights into a structural basis for the switching of calcipotriol to a receptor antagonist by further side chain modification. J. Med. Chem. 47 (2004) 1956-1961
    • (2004) J. Med. Chem. , vol.47 , pp. 1956-1961
    • Tocchini-Valentini, G.1    Rochel, N.2    Wurtz, J.M.3    Moras, D.4
  • 41
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin A., and Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1622-1624
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 42
    • 1842426936 scopus 로고    scopus 로고
    • Molecular strucutre of the rat vitamin D receptor ligand binding domain complexed with 2-carbon-substituted vitamin D3 hormone analogues and a LXXLL-containing coactivator peptide
    • Vanhooke J.L., Benning M.M., Bauer C.B., Pike J.W., and DeLuca H.F. Molecular strucutre of the rat vitamin D receptor ligand binding domain complexed with 2-carbon-substituted vitamin D3 hormone analogues and a LXXLL-containing coactivator peptide. Biochemistry 43 (2004) 4101-4110
    • (2004) Biochemistry , vol.43 , pp. 4101-4110
    • Vanhooke, J.L.1    Benning, M.M.2    Bauer, C.B.3    Pike, J.W.4    DeLuca, H.F.5
  • 44
    • 23844482445 scopus 로고    scopus 로고
    • Immunophenotypic changes induced on human HL60 leukaemia cells by 1α,25-dihydroxyvitamin D3 and 12-O-tetradecanoyl phorbol-13-acetate
    • White S.L., Belov L., Barber N., Hodgkin P.D., and Christopherson R.I. Immunophenotypic changes induced on human HL60 leukaemia cells by 1α,25-dihydroxyvitamin D3 and 12-O-tetradecanoyl phorbol-13-acetate. Leuk. Res. 29 (2005) 1141-1151
    • (2005) Leuk. Res. , vol.29 , pp. 1141-1151
    • White, S.L.1    Belov, L.2    Barber, N.3    Hodgkin, P.D.4    Christopherson, R.I.5
  • 45
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.