메뉴 건너뛰기




Volumn 74, Issue 3, 1999, Pages 323-333

Three-dimensional model of the ligand binding domain of the nuclear receptor for 1α,25-dihydroxy-vitamin D3

Author keywords

1 ,25(OH)2D3; Model; Nuclear receptor; Steroid receptor

Indexed keywords

CALCITRIOL; CELL NUCLEUS RECEPTOR; LIGAND; THYROID HORMONE RECEPTOR; VITAMIN D RECEPTOR;

EID: 0033197920     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(19990901)74:3<323::AID-JCB2>3.0.CO;2-V     Document Type: Article
Times cited : (37)

References (33)
  • 1
  • 3
    • 0028988403 scopus 로고
    • Structure-function relationships in the vitamin D endocrine system
    • Bouillon R, Okamura WH, Norman AW. 1995. Structure-function relationships in the vitamin D endocrine system. Endocr Rev 16:200-257.
    • (1995) Endocr Rev , vol.16 , pp. 200-257
    • Bouillon, R.1    Okamura, W.H.2    Norman, A.W.3
  • 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, Moras D. 1995. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. 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
  • 9
    • 0030949836 scopus 로고    scopus 로고
    • GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors
    • Hong H, Kohli K, Garabedian MJ, Stallcup MR. 1997. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol Cell Biol 17:2735-2744.
    • (1997) Mol Cell Biol , vol.17 , pp. 2735-2744
    • Hong, H.1    Kohli, K.2    Garabedian, M.J.3    Stallcup, M.R.4
  • 10
    • 0030980888 scopus 로고    scopus 로고
    • 3 receptor identifying C-terminal amino acids required for transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription factor IIB, in vitro
    • 3 receptor identifying C-terminal amino acids required for transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription factor IIB, in vitro. J Biol Chem 272:14592-14599.
    • (1997) J Biol Chem , vol.272 , pp. 14592-14599
    • Jurutka, P.W.1    Hsieh, J.C.2    Remus, L.S.3    Whitfield, G.K.4    Thompson, P.D.5    Haussler, C.A.6    Blanco, J.C.7    Ozato, K.8    Haussler, M.R.9
  • 13
    • 0031038088 scopus 로고    scopus 로고
    • Hereditary vitamin D resistant rickets caused by a novel mutation in the vitamin D receptor that results in decreased affinity for hormone and cellular hyporesponsiveness
    • Malloy PJ, Eccleshall TR, Gross C, Van Maldergem L, Bouillon R, Feldman D. 1997. Hereditary vitamin D resistant rickets caused by a novel mutation in the vitamin D receptor that results in decreased affinity for hormone and cellular hyporesponsiveness. J Clin Invest 99:297-304.
    • (1997) J Clin Invest , vol.99 , pp. 297-304
    • Malloy, P.J.1    Eccleshall, T.R.2    Gross, C.3    Van Maldergem, L.4    Bouillon, R.5    Feldman, D.6
  • 14
    • 0027370857 scopus 로고
    • Effect of C20 stereochemistry on the conformational profile of the side chains of vitamin D analogs
    • Midland MM, Plumet J, Okamura WH. 1993. Effect of C20 stereochemistry on the conformational profile of the side chains of vitamin D analogs. Bioorg Med Chem Lett 3:1799-1804.
    • (1993) Bioorg Med Chem Lett , vol.3 , pp. 1799-1804
    • Midland, M.M.1    Plumet, J.2    Okamura, W.H.3
  • 22
    • 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, Moras D. 1995. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378:681-689.
    • (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
  • 24
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tanenbaum DM, Wang Y, Williams SP, Sigler PB. 1998. Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci USA 95:5998-6003.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5998-6003
    • Tanenbaum, D.M.1    Wang, Y.2    Williams, S.P.3    Sigler, P.B.4
  • 28
    • 0029123088 scopus 로고
    • A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation
    • Whitfield GK, Hsieh JC, Nakajima S, MacDonald PN, Thompson PD, Jurutka PW, Haussler CA, Haussler MR. 1995. A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation. Mol Endocrinol 9:1166-1179.
    • (1995) Mol Endocrinol , vol.9 , pp. 1166-1179
    • Whitfield, G.K.1    Hsieh, J.C.2    Nakajima, S.3    MacDonald, P.N.4    Thompson, P.D.5    Jurutka, P.W.6    Haussler, C.A.7    Haussler, M.R.8
  • 30
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • Williams SP, Sigler PB. 1998. Atomic structure of progesterone complexed with its receptor. Nature 393:392-396.
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 31
    • 0001037347 scopus 로고    scopus 로고
    • 3D model of the ligand binding domain of the vitamin D nuclear receptor based on the crystal structure of holo RARγ
    • Norman AW, Bouillon R, Thomasset M, editors. Riverside, CA: University of California-Riverside Printing and Reprographics
    • Wurtz J-M, Guillot B, Moras D. 1997. 3D model of the ligand binding domain of the vitamin D nuclear receptor based on the crystal structure of holo RARγ. In: Norman AW, Bouillon R, Thomasset M, editors. Vitamin D: chemistry, biology and clinical applications of the steroid hormone. Riverside, CA: University of California-Riverside Printing and Reprographics, pp 165-172.
    • (1997) Vitamin D: Chemistry, Biology and Clinical Applications of the Steroid Hormone , pp. 165-172
    • Wurtz, J.-M.1    Guillot, B.2    Moras, D.3
  • 33
    • 0032560137 scopus 로고    scopus 로고
    • Conformation-function relationship of vitamin D: Conformational analysis predicts potential side-chain structure
    • Yamada S, Yamamoto K, Masuno H, Ohta M. 1998. Conformation-function relationship of vitamin D: conformational analysis predicts potential side-chain structure. J Med Chem 41:1467-1475.
    • (1998) J Med Chem , vol.41 , pp. 1467-1475
    • Yamada, S.1    Yamamoto, K.2    Masuno, H.3    Ohta, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.