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Thyroxine-Thyroid Hormone Receptor Interactions
Open accessAbstract
Thyroid hormone (TH) actions are mediated by nuclear receptors (TRs alpha and beta) that bind triiodothyronine (T(3), 3,5,3'-triiodo-l-thyronine) with high affinity, and its precursor thyroxine (T(4), 3,5,3',5'-tetraiodo-l-thyronine) with lower affinity. T(4) contains a bulky 5' iodine group absent from T(3). Because T(3) is buried in the core of the ligand binding domain (LBD), we have predicted that TH analogues with 5' substituents should fit poorly into the ligand binding pocket and perhaps behave as antagonists. We therefore examined how T(4) affects TR activity and conformation. We obtained several lines of evidence (ligand dissociation kinetics, migration on hydrophobic interaction columns, and non-denaturing gels) that TR-T(4) complexes adopt a conformation that differs from TR-T(3) complexes in solution. Nonetheless, T(4) behaves as an agonist in vitro (in effects on coregulator and DNA binding) and in cells, when conversion to T(3) does not contribute to agonist activity. We determined x-ray crystal structures of the TRbeta LBD in complex with T(3) and T(4) at 2.5-A and 3.1-A resolution. Comparison of the structures reveals that TRbeta accommodates T(4) through subtle alterations in the loop connecting helices 11 and 12 and amino acid side chains in the pocket, which, together, enlarge a niche that permits helix 12 to pack over the 5' iodine and complete the coactivator binding surface. While T(3) is the major active TH, our results suggest that T(4) could activate nuclear TRs at appropriate concentrations. The ability of TR to adapt to the 5' extension should be considered in TR ligand design.
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“The protein receptors bind T 3 with greater (>10Â) affinity than T 4 (8).”
From Thyroid Hormones and Cardiovascular Function and Diseases (2018) · cites this paper as [8]
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Raval, S., Raval, P., Bandyopadhyay, D., Soni, K., Yevale, D. B., Jogiya, D., Modi, H., Joharapurkar, A. A., Gandhi, N. S., Jain, M. R., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.06.038 · Cited by 8
Circulating thyroid hormones and clinical parameters of heart failure in men
Turić, I., Velat, I., Bušić, Ž., & Čulić, V. (2023) · Scientific Reports · doi:10.1038/s41598-023-47391-3 · Cited by 7
Bao, J., Jin, H., Wang, Y., Jin, J., & Chen, L. (2022) · Environment International · doi:10.1016/j.envint.2022.107390 · Cited by 7
Halogen bonds between ligands and proteins: Can we use them in validation?
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Lima, S. T. D. C., Nguyen, N.-H., Togashi, M., Apriletti, J. W., Nguyen, P. T., Polikarpov, I., Scanlan, T. S., Baxter, J. D., & Webb, P. (2009) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2009.08.003 · Cited by 6
The oligomeric state of thyroid receptor regulates hormone binding kinetics
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Heat conduction by thyroid hormone receptors
Lamichhane, T. R., & Lamichhane, H. P. (2018) · AIMS Biophysics · doi:10.3934/biophy.2018.4.245 · Cited by 6
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Thyroid Hormones (T3 and T4) and Their Effects on the Cardiovascular System
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Metadata
- Authors
- Sandler, B., Webb, P., Apriletti, J. W., Huber, B. R., Togashi, M., Lima, S. T. C., Juric, S., Nilsson, S., Wagner, R., Fletterick, R. J., & Baxter, J. D.
- Affiliations
- University of California, San Francisco (US)
- Karo Pharma (Sweden) (SE)
- Corresponding author
- Baxter, John D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-12
- Volume
- 279
- Issue
- 53
- Pages
- 55801-55808
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2170170098
- Cited by
- 152
- References
- 38
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 9 · 2023: 7 · 2022: 11 · 2021: 11 · 2020: 4 · 2019: 11 · 2018: 7 · 2017: 7 · 2016: 9 · 2015: 2 · 2014: 9 · 2013: 5 · 2012: 4
- FWCI
- 3.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Americanae (AECID Library) (submittedVersion)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK064148, DK41842, DK-64148, DK-58390, R01DK041842, P01DK058390)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Keywords
- thyroxine, triiodothyronine, thyroid hormone receptor beta, nuclear receptor ligand-binding domain, receptor conformation, ligand binding affinity, coactivator binding, receptor agonist activity, crystal structure, ligand design
- MeSH terms
- Animals, Chromatography, DNA, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Glutathione Transferase, Cricetinae, Iodine, Kinetics, Ligands, Models, Chemical, Models, Molecular, Protein Binding, Protein Conformation, Receptors, Thyroid Hormone, Thyroxine, Time Factors, Transfection, Triiodothyronine, CHO Cells, Protein Structure, Tertiary, Crystallography, X-Ray, Dimerization
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