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Structural aspects of thyroid hormone binding to proteins and competitive interactions with natural and synthetic compounds

Title data

Schweizer, Ulrich ; Towell, Holly ; Vit, Allegra ; Rodriguez-Ruiz, Alfonso ; Steegborn, Clemens:
Structural aspects of thyroid hormone binding to proteins and competitive interactions with natural and synthetic compounds.
In: Molecular and Cellular Endocrinology. Vol. 458 (2017) . - pp. 57-67.
ISSN 0303-7207
DOI: https://doi.org/10.1016/j.mce.2017.01.026

Abstract in another language

Thyroid hormones and their metabolites constitute a vast class of related iodothyronine compounds that contribute to the regulation of metabolic activity and cell differentiation. They are in turn transported, transformed and recognized as signaling molecules through binding to a variety of proteins from a wide range of evolutionary unrelated protein families, which renders these proteins and their iodothyronine binding sites an example for extensive convergent evolution. In this review, we will briefly summarize what is known about iodothyronine binding sites in proteins, the modes of protein/iodothyronine interaction, and the ligand conformations. We will then discuss physiological and synthetic compounds, including popular drugs and food components, that can interfere with iodothyronine binding and recognition by these proteins. The discussion also includes compounds persisting in the environment and acting as endocrine disrupting chemicals.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 29 Mar 2017 07:04
Last Modified: 21 Nov 2017 09:32
URI: https://eref.uni-bayreuth.de/id/eprint/36685