AUTHOR=Kleinau Gunnar , Worth Catherine L. , Kreuchwig Annika , Biebermann Heike , Marcinkowski Patrick , Scheerer Patrick , Krause Gerd TITLE=Structural–Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at Work JOURNAL=Frontiers in Endocrinology VOLUME=8 YEAR=2017 URL=https://www.frontiersin.org/journals/endocrinology/articles/10.3389/fendo.2017.00086 DOI=10.3389/fendo.2017.00086 ISSN=1664-2392 ABSTRACT=
The thyroid-stimulating hormone receptor (TSHR) is a member of the glycoprotein hormone receptors, a sub-group of class A G-protein-coupled receptors (GPCRs). TSHR and its endogenous ligand thyrotropin (TSH) are of essential importance for growth and function of the thyroid gland and proper function of the TSH/TSHR system is pivotal for production and release of thyroid hormones. This receptor is also important with respect to pathophysiology, such as autoimmune (including ophthalmopathy) or non-autoimmune thyroid dysfunctions and cancer development. Pharmacological interventions directly targeting the TSHR should provide benefits to disease treatment compared to currently available therapies of dysfunctions associated with the TSHR or the thyroid gland. Upon TSHR activation, the molecular events conveying conformational changes from the extra- to the intracellular side of the cell across the membrane comprise reception, conversion, and amplification of the signal. These steps are highly dependent on structural features of this receptor and its intermolecular interaction partners, e.g., TSH, antibodies, small molecules, G-proteins, or arrestin. For better understanding of signal transduction, pathogenic mechanisms such as autoantibody action and mutational modifications or for developing new pharmacological strategies, it is essential to combine available structural data with functional information to generate homology models of the entire receptor. Although so far these insights are fragmental, in the past few decades essential contributions have been made to investigate in-depth the involved determinants, such as by structure determination