Activation of nuclear receptors: A perspective from structural genomics

Structure

Volumn 11, Issue 7, 2003, Pages 741-746

  Li, Yong ^a   Lambert, Millard H ^b   Xu, H Eric ^a  

^a VAN ANDEL RESEARCH INSTITUTE   (United States)

^b GLAXOSMITHKLINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR;

CRYSTAL STRUCTURE; GENE ACTIVATION; GENE REPRESSION; GENOMICS; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION;

EID: 0038646966     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(03)00133-3     Document Type: Review

References (28)

1. Baker K.D., Shewchuk L.M., Kozlova T., Makishima M., Hassell A., Wisely B., Caravella J.A., Lambert M.H., Reinking J.L., Krause H.et al. The Drosophila orphan nuclear receptor DHR38 mediates an atypical ecdysteroid signaling pathway. Cell. 113:2003;731-742.
2. 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. Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell. 110:2002;93-105.
3. Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α Nature. 375:1995;377-382.
4. Brzozowski A.M., Pike A.C., Dauter Z., Hubbard R.E., Bonn T., Engstrom O., Ohman L., Greene G.L., Gustafsson J.A., Carlquist M. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 389:1997;753-758.
5. Chawla A., Repa J.J., Evans R.M., Mangelsdorf D.J. Nuclear receptors and lipid physiology. opening the X-files Science. 294:2001;1866-1870.
6. Dhe-Paganon, S., Duda, K., Iwamoto, M., Chi, Y.I., and Shoelson, S.E. (2002). Crystal structure of the HNF4α ligand binding domain in complex with endogenous fatty acid ligand. J. Biol. Chem. 277, 37973-37936.
7. Gampe R.T. Jr., Montana V.G., Lambert M.H., Miller A.B., Bledsoe R.K., Milburn M.V., Kliewer S.A., Willson T.M., Xu H.E. Asymmetry in the PPARγ/RXRα crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol. Cell. 5:2000;545-555. a.
8. Gampe R.T. Jr., Montana V.G., Lambert M.H., Wisely G.B., Milburn M.V., Xu H.E. Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix. Genes Dev. 14:2000;2229-2241. b.
9. Goodwin B., Jones S.A., Price R.R., Watson M.A., McKee D.D., Moore L.B., Galardi C., Wilson J.G., Lewis M.C., Roth M.E.et al. A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis. Mol. Cell. 6:2000;517-526.
10. Greschik H., Wurtz J.M., Sanglier S., Bourguet W., van Dorsselaer A., Moras D., Renaud J.P. Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol. Cell. 9:2002;303-313.
11. Kliewer S.A., Lehmann J.M., Willson T.M. Orphan nuclear receptors. shifting endocrinology into reverse Science. 284:1999;757-760.
12. Lu T.T., Makishima M., Repa J.J., Schoonjans K., Kerr T.A., Auwerx J., Mangelsdorf D.J. Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors. Mol. Cell. 6:2000;507-515.
13. NRNC A unified nomenclature system for the nuclear receptor superfamily. Cell. 97:1999;161-163.
14. Renaud J.P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., Moras D. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature. 378:1995;681-689.
15. Rosenfeld M.G., Glass C.K. Coregulator codes of transcriptional regulation by nuclear receptors. J. Biol. Chem. 276:2001;36865-36868.
16. Sablin E.P., Krylova I.N., Fletterick R.J., Ingraham H.A. Structural basis for ligand-independent activation of the orphan nuclear receptor LRH-1. Mol. Cell. 11:2003;1575-1585.
17. Schulman I.G., Shao G., Heyman R.A. Transactivation by retinoid X receptor-peroxisome proliferator-activated receptor γ (PPARγ) heterodimers. intermolecular synergy requires only the PPARγ hormone-dependent activation function Mol. Cell. Biol. 18:1998;3483-3494.
18. Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., Greene G.L. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell. 95:1998;927-937.
19. Soutoglou E., Katrakili N., Talianidis I. Acetylation regulates transcription factor activity at multiple levels. Mol. Cell. 5:2000;745-751.
20. Wagner R.L., Apriletti J.W., McGrath M.E., West B.L., Baxter J.D., Fletterick R.J. A structural role for hormone in the thyroid hormone receptor. Nature. 378:1995;690-697.
21. Wang Z., Benoit G., Liu J., Prasad S., Aarnisalo P., Liu X., Xu H., Walker N.P., Perlmann T. Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors. Nature. 423:2003;555-560.
22. Watkins R.E., Wisely G.B., Moore L.B., Collins J.L., Lambert M.H., Williams S.P., Willson T.M., Kliewer S.A., Redinbo M.R. The human nuclear xenobiotic receptor PXR. structural determinants of directed promiscuity Science. 292:2001;2329-2333.
23. Willson T.M., Moore J.T. Genomics versus orphan nuclear receptors - a half-time report. Mol. Endocrinol. 16:2002;1135-1144.
24. Wisely G.B., Miller A.B., Davis R.G., Thornquest A.D. Jr., Johnson R., Spitzer T., Sefler A., Shearer B., Moore J.T., Willson T.M.et al. Hepatocyte nuclear factor 4 is a transcription factor that constitutively binds fatty acids. Structure. 10:2002;1225-1234.
25. Xu H.E., Lambert M.H., Montana V.G., Parks D.J., Blanchard S.G., Brown P.J., Sternbach D.D., Lehmann J.M., Wisely G.B., Willson T.M.et al. Molecular recognition of fatty acids by peroxisome proliferator-activated receptors. Mol. Cell. 3:1999;397-403.
26. Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B., Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D.et al. Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc. Natl. Acad. Sci. USA. 98:2001;13919-13924.
27. Xu H.E., Stanley T.B., Montana V.G., Lambert M.H., Shearer B.G., Cobb J.E., McKee D.D., Galardi C.M., Plunket K.D., Nolte R.T.et al. Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARα Nature. 415:2002;813-817.
28. Zetterstrom R.H., Solomin L., Jansson L., Hoffer B.J., Olson L., Perlmann T. Dopamine neuron agenesis in Nurr1-deficient mice. Science. 276:1997;248-250.