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Mol Cell Endocrinol. 2017 Dec 15;458:57-67. doi: 10.1016/j.mce.2017.01.026. Epub 2017 Jan 25.

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

Author information

1
Institut für Biochemie und Molekularbiologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany. Electronic address: Ulrich.schweizer@uni-bonn.de.
2
Lehrstuhl für Biochemie, Universität Bayreuth, Bayreuth, Germany.
3
Institut für Biochemie und Molekularbiologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany.
4
Lehrstuhl für Biochemie, Universität Bayreuth, Bayreuth, Germany. Electronic address: Clemens.Steegborn@uni-bayreuth.de.

Abstract

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.

KEYWORDS:

Binding site; Complex; Drug; Iodothyronine; Ligand conformation

PMID:
28131741
DOI:
10.1016/j.mce.2017.01.026
[Indexed for MEDLINE]

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