Spatial requirement for coupling of iodotyrosine residues to form thyroid hormones.
Open accessAbstract
A linear random copolymer of tyrosine and lysine and two synthetic oligopeptides containing two tyrosine residues in addition to lysine residues give thyroid hormone (thyroxine and triodothyronine) residues in good yield upon enzymatic iodination with thyroid peroxidase. These synthetic peptides may serve as simple models for thyroglobulin, the protein in which biosynthesis of the thyroid hormone takes place. For the formation of significant amounts of hormone, such model compounds must contain at least two properly spaced tyrosine residues.
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The lack of a three-dimensional structure of TG has prevented mechanistic understanding.
“hormonogenic tyrosines have not been clearly identified and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4.”
From The structure of human thyroglobulin (2020) · cites this paper as [4]
The introductory passage (page unavailable) says thyroglobulin’s primary sequence was unknown and the molecule was too complex to study the factors governing spatial alignment, prompting the authors to use simpler models. It does not specifically say that the lack of a three-dimensional structure prevented mechanistic understanding more broadly. (LLM, conf=0.82)
Experimental — accuracy not yet measuredHormonogenic tyrosines in thyroglobulin have not been clearly identified.
“hormonogenic tyrosines have not been clearly identified and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4.”
From The structure of human thyroglobulin (2020) · cites this paper as [4]
The introductory passage (page not supplied) says thyroglobulin’s primary sequence was unknown and that its complexity prevented study of factors governing coupling. This is consistent with hormonogenic tyrosines not being clearly identified, but the paper does not specifically attribute the mechanistic limitation to a lack of three-dimensional structure. (LLM, conf=0.82)
Experimental — accuracy not yet measuredWith the ELISA, modest T4 synthesis could also be obtained from random tyrosine copolymers, as previously reported.
“Finally, with our ELISA we could also obtain modest T4 synthesis from random tyrosine copolymers, as previously reported4 (Extended Data Figure 6e).”
From The structure of human thyroglobulin (2020) · cites this paper as [4]
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Research works printed but not linked: 2
- Vassart, G., Refetoff, S., Brocas, H., Dinsart, C. & Dumont, J. E. (1975) "Translation of thyroglobulin 33S messenger RNA as a means of determining thyroglobulin quaternary structure," Proc. Natl. Acad. Sci. USA 72, 3839–3843.
- [10]Johnson, T. B. & Tewkesbury, L. B., Jr. (1942) "The oxidation of 3,5-diiodotyrosine to thyroxine,"Proc. Natl. Acad. Sci. USA
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The structure of human thyroglobulin
Coscia, F., Taler-Verčič, A., Chang, V. T., Sinn, L., O’Reilly, F. J., Izoré, T., Renko, M., Berger, I., Rappsilber, J., Turk, D., et al. (2020) · Nature · doi:10.1038/s41586-020-1995-4 · Cited by 147 · see citing works
- Authors
- Cahnmann, H. J., Pommier, J., & Nunez, J.
- Affiliations
- National Institutes of Health (US)
- ORCID
- Nunez, J
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1977-12
- Volume
- 74
- Issue
- 12
- Pages
- 5333-5335
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC431707
- OpenAlex
- W2028480431
- Cited by
- 45
- References
- 0
- Citations by year
- 2026: 1 · 2024: 2 · 2022: 1 · 2020: 2 · 2019: 2 · 2018: 1 · 2017: 2 · 2016: 3 · 2015: 1 · 2014: 1
- FWCI
- 1.18
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- thyroid hormone synthesis, thyroxine, triiodothyronine, thyroid peroxidase, synthetic oligopeptides
- MeSH terms
- Iodide Peroxidase, Iodides, Models, Biological, Peptides, Structure-Activity Relationship, Thyroglobulin, Thyroid Gland, Thyroid Hormones, Tyrosine
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