Structural basis for negative cooperativity within agonist-bound TR:RXR heterodimers

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 16, 2012, Pages 6084-6087

  Putcha, Balananda Dhurjati K ^a   Wright, Edward ^a   Brunzelle, Joseph S ^b   Fernandez, Elias J ^a  

^a UNIVERSITY OF TENNESSEE   (United States)

^b NORTHWESTERN UNIVERSITY   (United States)

Author keywords

Allostery; Thyroid receptor

Indexed keywords

HETERODIMER; LIOTHYRONINE; RETINOIC ACID RECEPTOR; STEROID RECEPTOR COACTIVATOR 1; THYROID HORMONE RECEPTOR;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; BINDING KINETICS; CHEMICAL STRUCTURE; LIGAND BINDING; LIPOGENESIS; PRIORITY JOURNAL; TRANSACTIVATION;

ANIMALS; BINDING SITES; BINDING, COMPETITIVE; CALORIMETRY; CELL LINE; CRYSTALLOGRAPHY, X-RAY; HUMANS; KINETICS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RETINOID X RECEPTORS; THYROID HORMONE RECEPTORS ALPHA; TRIIODOTHYRONINE;

EID: 84859982562     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1119852109     Document Type: Article

References (30)

1. Forman BM, Umesono K, Chen J, Evans RM (1995) Unique response pathways are established by allosteric interactions among nuclear hormone receptors. Cell 81:541-550.
2. Shulman AI, Larson C, Mangelsdorf DJ, Ranganathan R (2004) Structural determinants of allosteric ligand activation in RXR heterodimers. Cell 116:417-429. (Pubitemid 38366318)
3. Putcha BD, Fernandez EJ (2009) Direct interdomain interactions can mediate allosterism in the thyroid receptor. J Biol Chem 284:22517-22524.
4. Schulman IG, Li C, Schwabe JW, Evans RM (1997) The phantom ligand effect: Allosteric control of transcription by the retinoid X receptor. Genes Dev 11:299-308. (Pubitemid 27079908)
5. Mangelsdorf DJ, Evans RM (1995) The RXR heterodimers and orphan receptors. Cell 83:841-850. (Pubitemid 26006526)
6. Mengeling BJ, Lee S, Privalsky ML (2008) Coactivator recruitment is enhanced by thyroid hormone receptor trimers. Mol Cell Endocrinol 280:47-62. (Pubitemid 350184201)
7. Westin S, et al. (1998) Interactions controlling the assembly of nuclear-receptor heterodimers and co-activators. Nature 395:199-202. (Pubitemid 28425662)
8. Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D (1995) Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature 375: 377-382.
9. Xu HE, et al. (2002) Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha. Nature 415:813-817. (Pubitemid 34150506)
10. Shan L, et al. (2004) Structure of the murine constitutive androstane receptor complexed to androstenol: A molecular basis for inverse agonism. Mol Cell 16:907-917. (Pubitemid 40018401)
11. Egea PF, et al. (2000) Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid. EMBO J 19:2592-2601. (Pubitemid 30323548)
12. Ribeiro RC, et al. (1995) The molecular biology of thyroid hormone action. Ann N Y Acad Sci 758:366-389.
13. Yen PM (2001) Physiological and molecular basis of thyroid hormone action. Physiol Rev 81:1097-1142.
14. Wagner RL, et al. (1995) A structural role for hormone in the thyroid hormone receptor. Nature 378:690-697.
15. Artymiuk PJ, et al. (1979) Crystallographic studies of the dynamic properties of lysozyme. Nature 280:563-568.
16. Huber R (1987) Flexibility and rigidity, requirements for the function of proteins and protein pigment complexes. Eleventh Keilin memorial lecture. Biochem Soc Trans 15: 1009-1020.
17. Carroll MJ, et al. (2011) Direct detection of structurally resolved dynamics in a multiconformation receptor-ligand complex. J Am Chem Soc 133:6422-6428.
18. Williams DH, O'Brien DP, Sandercock AM, Stephens E (2004) Order changes within receptor systems upon ligand binding: Receptor tightening/oligomerisation and the interpretation of binding parameters. J Mol Biol 340:373-383. (Pubitemid 38759916)
19. Lusher SJ, et al. (2011) Structural basis for agonism and antagonism for a set of chemically related progesterone receptor modulators. J Biol Chem 286:35079-35086.
20. Jeyakumar M, Webb P, Baxter JD, Scanlan TS, Katzenellenbogen JA (2008) Quantification of ligand-regulated nuclear receptor corepressor and coactivator binding, key interactions determining ligand potency and efficacy for the thyroid hormone receptor. Biochemistry 47:7465-7476. (Pubitemid 351991025)
21. Huber BR, et al. (2003) Two resistance to thyroid hormone mutants with impaired hormone binding. Mol Endocrinol 17:643-652. (Pubitemid 36403576)
22. Moore JM, Guy RK (2005) Coregulator interactions with the thyroid hormone receptor. Mol Cell Proteomics 4:475-482. (Pubitemid 40590566)
23. Wright E, et al. (2011) Helix 11 dynamics is critical for constitutive androstane receptor activity. Structure 19:37-44.
24. Bourguet W, et al. (2000) Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol Cell 5:289-298. (Pubitemid 30628087)
25. Suino K, et al. (2004) The nuclear xenobiotic receptor CAR: Structural determinants of constitutive activation and heterodimerization. Mol Cell 16:893-905. (Pubitemid 40018400)
26. Nascimento AS, et al. (2006) Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function. J Mol Biol 360: 586-598. (Pubitemid 43975107)
27. Arsanjani R, McCarren M, Bahl JJ, Goldman S (2011) Translational potential of thyroid hormone and its analogs. J Mol Cell Cardiol 51:506-511.
28. Refetoff S, Dumitrescu AM (2007) Syndromes of reduced sensitivity to thyroid hormone: Genetic defects in hormone receptors, cell transporters and deiodination. Best Pract Res Clin Endocrinol Metab 21:277-305. (Pubitemid 46888195)
29. de Urquiza AM, et al. (2000) Docosahexaenoic acid, a ligand for the retinoid X receptor in mouse brain. Science 290:2140-2144.
30. Volakakis N, Joodmardi E, Perlmann T (2009) NR4A orphan nuclear receptors influence retinoic acid and docosahexaenoic acid signaling via up-regulation of fatty acid binding protein 5. Biochem Biophys Res Commun 390:1186-1191.