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Volumn 43, Issue 14, 2004, Pages 4101-4110

Molecular Structure of the Rat Vitamin D Receptor Ligand Binding Domain Complexed with 2-Carbon-Substituted Vitamin D3 Hormone Analogues and A LXXLL-Containing Coactivator Peptide

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CRYSTAL STRUCTURE; ELECTROSTATICS; HYDROGEN BONDS; HYDROPHOBICITY; HYDROXYLATION; TERNARY SYSTEMS; VITAMINS; WATER;

EID: 1842426936     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036056y     Document Type: Article
Times cited : (192)

References (50)
  • 1
    • 0031755168 scopus 로고    scopus 로고
    • Current understanding of the molecular actions of vitamin D
    • Jones, G., Strugnell, S. A., and DeLuca, H. F. (1998) Current understanding of the molecular actions of vitamin D, Physiol. Rev. 78, 1193-1231.
    • (1998) Physiol. Rev. , vol.78 , pp. 1193-1231
    • Jones, G.1    Strugnell, S.A.2    DeLuca, H.F.3
  • 4
    • 0020265220 scopus 로고
    • 1α,25-dihydroxycholecalciferol and a human myeloid leukemia cell line (HL-60)
    • Tanaka, H., Abe, E., Miyaura, C., Kuribayashi, T., Konno, K., Nishii, Y., and Suda, T. (1982) 1α,25-Dihydroxycholecalciferol and a human myeloid leukemia cell line (HL-60), Biochem. J. 204, 713-719.
    • (1982) Biochem. J. , vol.204 , pp. 713-719
    • Tanaka, H.1    Abe, E.2    Miyaura, C.3    Kuribayashi, T.4    Konno, K.5    Nishii, Y.6    Suda, T.7
  • 6
    • 0022621042 scopus 로고
    • 3 on the morphologic and biochemical differentiation of cultured human epidermal keratinocytes grown in serum-free conditions
    • 3 on the morphologic and biochemical differentiation of cultured human epidermal keratinocytes grown in serum-free conditions, J. Invest. Dermatol. 86, 709-714.
    • (1986) J. Invest. Dermatol. , vol.86 , pp. 709-714
    • Smith, E.L.1    Walworth, N.C.2    Holick, M.F.3
  • 7
    • 0002628959 scopus 로고    scopus 로고
    • Vitamin D and renal failure
    • (Feldman, D., Glorieux, F. H., and Pike, J. W., Eds.), Academic Press, San Diego, CA
    • Slatopolski, E. S., and Brown, A. J. (1997) Vitamin D and renal failure, in Vitamin D (Feldman, D., Glorieux, F. H., and Pike, J. W., Eds.) pp 849-865, Academic Press, San Diego, CA.
    • (1997) Vitamin D , pp. 849-865
    • Slatopolski, E.S.1    Brown, A.J.2
  • 8
    • 0015929252 scopus 로고
    • Pathogenesis of hereditary vitamin D-dependent rickets. An inborn error of vitamin D metabolism involving defective conversion of 25-hydroxyvitamin D to 1α,25-dihydroxyvitamin D
    • Fraser, D., Kooh, S. W., Kind, H. P., Holick, M. F., Tanaka, Y., and DeLuca, H. F. (1973) Pathogenesis of hereditary vitamin D-dependent rickets. An inborn error of vitamin D metabolism involving defective conversion of 25-hydroxyvitamin D to 1α,25-dihydroxyvitamin D, N. Engl. J. Med. 289, 817-822.
    • (1973) N. Engl. J. Med. , vol.289 , pp. 817-822
    • Fraser, D.1    Kooh, S.W.2    Kind, H.P.3    Holick, M.F.4    Tanaka, Y.5    DeLuca, H.F.6
  • 9
    • 0018932838 scopus 로고
    • Bone response to phosphate salts, ergocalciferol, and calcitriol in hypophosphatemic vitamin D-resistant rickets
    • Glorieux, F. H., Marie, P. J., Pettifor, J. M., and Delvin, E. E. (1980) Bone response to phosphate salts, ergocalciferol, and calcitriol in hypophosphatemic vitamin D-resistant rickets, N. Engl. J. Med. 303, 1023-1031.
    • (1980) N. Engl. J. Med. , vol.303 , pp. 1023-1031
    • Glorieux, F.H.1    Marie, P.J.2    Pettifor, J.M.3    Delvin, E.E.4
  • 10
    • 0001946211 scopus 로고    scopus 로고
    • Clinical disorders of phosphate homeostasis
    • (Feldman, D., Glorieux, F. H., and Pike, J. W., Eds.), Academic Press, San Diego, CA
    • Drezner, M. K. (1997) Clinical disorders of phosphate homeostasis, in Vitamin D (Feldman, D., Glorieux, F. H., and Pike, J. W., Eds.) pp 733-753, Academic Press, San Diego, CA.
    • (1997) Vitamin D , pp. 733-753
    • Drezner, M.K.1
  • 11
    • 0025997260 scopus 로고
    • Is there a role for vitamin D in osteoporosis?
    • Lamberg-Allardt, C. (1991) Is there a role for vitamin D in osteoporosis? Calcif. Tissue Int. 49 (Suppl.), S46-49.
    • (1991) Calcif. Tissue Int. , vol.49 , Issue.SUPPL.
    • Lamberg-Allardt, C.1
  • 12
    • 0027193402 scopus 로고
    • Topical calcitriol in the treatment of chronic plaque psoriasis: A double-blind study
    • Langner, A., Verjans, H., Stapor, V., Moli, M., and Fraczykowska, M. (1993) Topical calcitriol in the treatment of chronic plaque psoriasis: a double-blind study, Br. J. Dermatol. 128, 566-571.
    • (1993) Br. J. Dermatol. , vol.128 , pp. 566-571
    • Langner, A.1    Verjans, H.2    Stapor, V.3    Moli, M.4    Fraczykowska, M.5
  • 13
    • 0034532265 scopus 로고    scopus 로고
    • Vitamin D: A natural inhibitor of multiple sclerosis
    • Hayes, C. E. (2000) Vitamin D: a natural inhibitor of multiple sclerosis, Proc. Nutr. Soc. 59, 531-535.
    • (2000) Proc. Nutr. Soc. , vol.59 , pp. 531-535
    • Hayes, C.E.1
  • 16
  • 17
    • 0001013226 scopus 로고
    • Phase II trial of oral 1,25-dihydroxyvitamin D (calcitriol) in hormone refractory prostate cancer
    • Osborn, J. L., Schwartz, G. G., Smith, D. C., Bahnson, R., Day, R., and Trump, D. L. (1995) Phase II trial of oral 1,25-dihydroxyvitamin D (calcitriol) in hormone refractory prostate cancer, Urol. Oncol. 1, 195-198.
    • (1995) Urol. Oncol. , vol.1 , pp. 195-198
    • Osborn, J.L.1    Schwartz, G.G.2    Smith, D.C.3    Bahnson, R.4    Day, R.5    Trump, D.L.6
  • 18
    • 0028988403 scopus 로고
    • Structure-function relationships in the vitamin D endocrine system
    • Bouillon, R., Okamura, W. H., and Norman, A. W. (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
  • 19
    • 0023235265 scopus 로고
    • Structures and biological activities of vitamin D metabolites and their analogs
    • Ikekawa, N. (1987) Structures and biological activities of vitamin D metabolites and their analogs, Med. Res. Rev. 7, 333-366.
    • (1987) Med. Res. Rev. , vol.7 , pp. 333-366
    • Ikekawa, N.1
  • 20
    • 0035342669 scopus 로고    scopus 로고
    • History of the development of new vitamin D analogs: Studies on 22-oxacalcitriol (OCT) and 2β-(3-hydroxypropoxy)calcitriol (ED-71)
    • Nishii, Y., and Okano, T. (2001) History of the development of new vitamin D analogs: studies on 22-oxacalcitriol (OCT) and 2β -(3-hydroxypropoxy)calcitriol (ED-71), Steroids 66, 137-146.
    • (2001) Steroids , vol.66 , pp. 137-146
    • Nishii, Y.1    Okano, T.2
  • 21
    • 0032487676 scopus 로고    scopus 로고
    • 3 compounds of high biological activity: Synthesis and biological evaluation of 2-hydroxymethyl, 2-methyl, and 2-methylene analogues
    • 3 compounds of high biological activity: synthesis and biological evaluation of 2-hydroxymethyl, 2-methyl, and 2-methylene analogues, J. Med. Chem. 41, 4662-4674.
    • (1998) J. Med. Chem. , vol.41 , pp. 4662-4674
    • Sicinski, R.R.1    Prahl, J.M.2    Smith, C.M.3    DeLuca, H.F.4
  • 25
    • 0026077212 scopus 로고
    • Baculovirus-mediated expression of the human vitamin D receptor. Functional characterization, vitamin D response element interactions, and evidence for a receptor auxiliary factor
    • MacDonald, P. N., Haussler, C. A., Terpening, C. M., Galligan, M. A., Reeder, M. C., Whitfield, G. K., and Haussler, M. R. (1991) Baculovirus-mediated expression of the human vitamin D receptor. Functional characterization, vitamin D response element interactions, and evidence for a receptor auxiliary factor, J. Biol. Chem. 266, 18808-18813.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18808-18813
    • MacDonald, P.N.1    Haussler, C.A.2    Terpening, C.M.3    Galligan, M.A.4    Reeder, M.C.5    Whitfield, G.K.6    Haussler, M.R.7
  • 26
    • 0031149846 scopus 로고    scopus 로고
    • 3 dependency of vitamin D receptor-retinoid X receptor-vitamin D-responsive element complex formation
    • 3 dependency of vitamin D receptor-retinoid X receptor-vitamin D-responsive element complex formation, Arch. Biochem. Biophys. 341, 75-80.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 75-80
    • Kimmel-Jehan, C.1    Jehan, F.2    DeLuca, H.F.3
  • 27
    • 0030771215 scopus 로고    scopus 로고
    • Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction
    • Masuyama, H., Brownfield, C. M., St-Arnaud, R., and MacDonald, P. N. (1997) Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction, Mol. Endocrinol. 11, 1507-1517.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1507-1517
    • Masuyama, H.1    Brownfield, C.M.2    St-Arnaud, R.3    MacDonald, P.N.4
  • 28
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-gamma 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. (1995) Crystal structure of the RAR-gamma 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
  • 29
    • 0034603725 scopus 로고    scopus 로고
    • 3 receptor: A network of coactivator interactions
    • 3 receptor: a network of coactivator interactions, Gene 246, 9-21.
    • (2000) Gene , vol.246 , pp. 9-21
    • Rachez, C.1    Freedman, L.P.2
  • 31
    • 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. (2000) The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand, Mol. Cell 5, 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
  • 33
    • 0034034013 scopus 로고    scopus 로고
    • The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes
    • Rachez, C., Gamble, M., Chang, C. P., Atkins, G. B., Lazar, M. A., and Freedman, L. P. (2000) The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes, Mol. Cell. Biol. 20, 2718-2726.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2718-2726
    • Rachez, C.1    Gamble, M.2    Chang, C.P.3    Atkins, G.B.4    Lazar, M.A.5    Freedman, L.P.6
  • 34
    • 0004482369 scopus 로고
    • 3 receptor on sodium dodecyl sulfate/polyacrylamide gels by renaturation and immunoblotting
    • 3 receptor on sodium dodecyl sulfate/polyacrylamide gels by renaturation and immunoblotting, Proc. Natl. Acad. Sci. U.S.A. 82, 7825-7829.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 7825-7829
    • Dame, M.C.1    Pierce, E.A.2    DeLuca, H.F.3
  • 35
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr., Sect. D 50, 760-763.
    • (1994) Acta Crystallogr., Sect. D , vol.50 , pp. 760-763
  • 36
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement, J. Appl. Crystallogr. 30, 1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 37
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr., Sect. D 53, 240-255.
    • (1997) Acta Crystallogr., Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 39
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structure coordinates
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structure coordinates, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. (1976) A solution for the best rotation to relate two sets of vectors, Acta Crystallogr., Sect. A 32, 922-923.
    • (1976) Acta Crystallogr., Sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 42
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B., and Richards, F. M. (1971) The interpretation of protein structures: estimation of static accessibility, J. Mol. Biol. 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 43
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia, C. (1975) Structural invariants in protein folding, Nature 254, 304-308.
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 46
    • 0000701094 scopus 로고
    • Vitamin D: Concerning the relationship between molecular topology and biological function
    • Okamura, W. H., Norman, A. W., and Wing, R. M. (1974) Vitamin D: concerning the relationship between molecular topology and biological function, Proc. Natl. Acad. Sci. U.S.A. 71, 4194-4197.
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 4194-4197
    • Okamura, W.H.1    Norman, A.W.2    Wing, R.M.3
  • 47
    • 0030950531 scopus 로고    scopus 로고
    • AF-2 activity and recruitment of steroid receptor coactivator-1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors
    • Henttu, P. M., Kalkhoven, E., and Parker, M. G. (1997) AF-2 activity and recruitment of steroid receptor coactivator-1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors, Mol. Cell. Biol. 17, 1832-1839.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1832-1839
    • Henttu, P.M.1    Kalkhoven, E.2    Parker, M.G.3
  • 48
    • 0027941792 scopus 로고
    • Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: Presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity
    • Durand, B., Saunders, M., Gaudon, C., Roy, B., Losson, R., and Chambon, P. (1994) Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity, EMBO J. 13, 5370-5382.
    • (1994) EMBO J. , vol.13 , pp. 5370-5382
    • Durand, B.1    Saunders, M.2    Gaudon, C.3    Roy, B.4    Losson, R.5    Chambon, P.6
  • 49
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha
    • Bourguet, W., Ruff, M., Chambon, P., Gronemeyer, H., and Moras, D. (1995) Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha, 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


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