Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand: 9-cis retinoic acid

EMBO Journal

Volumn 19, Issue 11, 2000, Pages 2592-2601

  Egea, Pascal F ^a   Mitschler, André ^a   Rochel, Natacha ^a   Ruff, Marc ^a   Chambon, Pierre ^a   Moras, Dino ^a  

^a CNRS   (France)

Author keywords

Conformational change; Crystal structure; Nuclear receptors; Retinoic acid; RXR

Indexed keywords

ALITRETINOIN; RETINOIC ACID RECEPTOR; RETINOID X RECEPTOR;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; LIGAND BINDING; PRIORITY JOURNAL; SIGNAL TRANSDUCTION;

APOPROTEINS; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HUMANS; LIGANDS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTORS, RETINOIC ACID; RECOMBINANT FUSION PROTEINS; RETINOID X RECEPTORS; STEREOISOMERISM; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTORS; TRETINOIN;

EID: 0034213831     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (41)

1. Allegretto, E.A. et al. (1993) Transactivation properties of retinoic acid and retinoid X receptor in mammalian cells and yeast. J. Biol. Chem., 268, 26625-26633.
2. Allenby, G. et al. (1993) Retinoic acid receptors and retinoid X receptors: interactions with endogenous retinoic acid. Proc. Natl Acad. Sci. USA, 90, 30-34.
3. Blondel, A., Renaud, J.-P., Fischer, S., Moras, D. and Karplus, M. (1999) Retinoic acid receptor: a simulation analysis of retinoic acid binding and the resulting conformational changes. J. Mol. Biol., 291, 101-115.
4. Botling, J., Castro, D.S., Öberg, F., Nilsson, K. and Perlmann, T. (1997) Retinoic acid receptor/retirnoid X receptor heterodimers can be activated through both subunits providing a basis for synergistic transactivation and cellular differentiation. J. Biol. Chem., 272, 9443-9449.
5. Bourguet, W., Ruff, M., Chambon, P., Gronemeyer, H. and Moras, D. (1995) Crystal structure of the ligand binding domain of the human nuclear receptor RXRα. Nature, 375, 377-382.
6. Bourguet, W., Vivat, V., Wurtz, J.-M., Chambon, P., Gronemeyer, H. and Moras, D. (2000) Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding-domains. Mol. Cell, 5, 289-298.
7. Brünger, A.T. (1998) Crystallography and NMR system: a new software for macromolecular structure determination. Acta Crystallogr. D, 54, 905-921.
8. Brzozowski, A.M. et al. (1997) Molecular basis of agonism and antagonism in the oestrogen receptor. Nature, 389, 753-758.
9. Chambon, P. (1996) A decade of molecular biology of retinoic acid receptors. FASEB J., 10, 940-954.
10. Darimont, B.D., Wagner, R.L., Apriletti, J.W., Stallcup, M.R., Kushner, P.J., Fletterick, R.J. and Yamamoto, K.R. (1998) Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev., 12, 3343-3356.
11. Dilworth, D.J., Fromental-Ramain, C., Remboutsika, E., Benecke, A. and Chambon, P. (1999) Ligand dependent activation of transcription in vitro by retinoic acid receptor α/retinoid X receptor α heterodimers that mimics transactivation by retinoids in vivo. Proc. Natl Acad. Sci. USA, 96, 1995-2000.
12. Ekena, K., Weis, K.E., Katzenellenbogen, J.A. and Katzenellenbogen, B.S. (1997) Different residues of the human estrogen receptor are involved in the recognition of structurally diverse estrogens and antiestrogens. J. Biol. Chem., 272, 5069-5075.
13. Gronemeyer, H. and Laudet, V. (1995) Introduction. In Sheterline, P. (ed.), Protein Profile: Transcription Factors 3: Nuclear Receptors. Academic Press, Liverpool, UK, pp. 1173-1181.
14. Heyman, R.A., Mangelsdorf, D.J., Dyck, J.A., Stein, R.B., Eichele, G., Evans, R.M. and Thaller, C. (1992) 9-cis retinoic acid is a high affinity ligand for the retinoid X receptor. Cell, 68, 397-406.
15. Jones, T.A., Zou, J.Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
16. Kastner, P., Mark, M. and Chambon, P. (1995) Non-steroid nuclear receptors: What are genetic studies telling us about their role in real life? Cell, 83, 859-869.
17. Klaholz, B.P., Renaud, J.-P., Mitschler, A., Zusi, C., Chambon, P., Gronemeyer, H. and Moras, D. (1998) Conformational adaptation of agonists to the human nuclear receptor RARγ. Nature Struct. Biol., 5, 199-202.
18. Kleywegt, G.J. and Jones, T.A. (1994) Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr. D, 50, 178-185.
19. 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.
20. Leid, M., Kastner, P. and Chambon, P. (1992) Multiplicity generates diversity in the retinoic acid signalling pathways Trends Biochem. Sci., 17, 427-433.
21. Levin, A.A. et al. (1992) 9-cis retinoic acid stereoisomer binds and activates the nuclear receptor RXRα. Nature, 355, 359-361.
22. Mangelsdorf, D.J., Umesono, K. and Evans, R.M. (1994) The retinoids receptors. In Sporn, M.B., Roberts, A.B. and Goodman, D.S. (eds), The Retinoids: Biology, Chemistry and Medicine. Raven Press, New York, NY, pp. 319-349.
23. Mangelsdorf, D.J. et al. (1995) The nuclear receptor superfamily: the second decade. Cell, 83, 835-839.
24. Minucci, S. et al. (1997) Retinoid X receptor RXR within the RXR retinoic acid receptor heterodimer binds its ligand and enhances retinoid dependent gene expression. Mol. Cell. Biol, 17, 644-655.
25. Moras, D. and Gronemeyer, H. (1998) The nuclear receptor ligand binding domain: structure and function. Curr. Opin. Cell Biol., 10, 384-391.
26. Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr. A, 50, 157-163.
27. Navaza, J. and Vernoslova, E. (1995) On the fast translation functions for molecular replacement. Acta Crystallogr. A, 51, 445-449.
28. Nolte, R.T. et al. (1998) Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ. Nature, 395, 137-143.
29. Otwinowski, Z. and Minor, W. ( 1996) Processing X-ray data collected in oscillation mode. Methods Enzymol., 276, 307-326.
30. Peet, D.J., Doyle, D.F., Corey, D.R. and Mangelsdorf, D.J. (1998) Engineering novel specificities for ligand-activated transcription in the nuclear hormone receptor RXR. Chem. Biol., 5, 13-21.
31. Philippsen, A. (1999) DINO: visualizing structural biology. http:// www.bioz.unibas.ch/∼xray/dino
32. Renaud, J.-P., Rochel, N., Ruff, M., Vivat, V., Chambon, P., Gronemeyer, H. and Moras, D. (1995) Crystal structure of the RARγ ligand binding domain bound to all-trans retinoic acid. Nature, 378, 681-689.
33. 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.
34. Shiau, A.K., Barstad, D., Loria, P.M., Cheng, L., Kushner, P.J., Agard, D.A. and Greene, G.L. (1998) The structural basis of estrogen receptor/ coactivator recognition and the antagonism of this interaction by tamoxifen. Cell, 95, 927-937.
35. Torchia, J., Glass C. and Rosenfeld M.G. (1998) Co-activators and corepressors in the integration of transcriptional responses. Curr. Opin. Cell Biol., 10, 373-383.
36. Umemiya, H. et al. (1997a) Action mechanism of retinoid-synergistic dihenzodiazepines. Biochem. Biophys. Res. Commun., 233, 121-125.
37. Umemiya, H. et al. (1997b) Regulation of retinoidal actions by diazepinylbenzoic acids. Retinoid synergists which activate the RXR-RAR heterodimers. J. Med. Chem., 40, 4222-4234.
38. Vivat, V. et al. (1997) A mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers. EMBO J., 16, 5697-5709.
39. Wagner, R.L., Apriletti, J.W., McGrath, M.E., West, B.L., Baxter, J.D. and Fletterick, R.J. (1995) A structural role for hormone in the thyroid hormone receptor. Nature, 378, 690-697.
40. Williams, S.P. and Sigler, P.B. (1998) Atomic structure of progesterone complexed with its receptor. Nature, 393, 392-396.
41. Wurtz, J.-M., Bourguet, W., Renaud, J.-P., Vivat, V., Chambon, P., Moras, D. and Gronemeyer, H. (1996) A canonical structure for the ligand binding domain of nuclear receptors. Nature Struct. Biol., 3, 87-94.