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. 2017 Apr 24;8:86. doi: 10.3389/fendo.2017.00086

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Copyright © 2017 Kleinau, Worth, Kreuchwig, Biebermann, Marcinkowski, Scheerer and Krause.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Scheme of the putative overall thyroid-stimulating hormone receptor (TSHR) protein structure. This scheme shows the overall structure and domain assembly of the TSHR. Significant features are highlighted, e.g., the sulfated tyrosine in the hinge region that is involved in hormone binding. The leucine-rich repeat domain (LRRD) together with the hinge region constituting the extracellular receptor part. The seven transmembrane helices and their connecting loops arrange the serpentine domain, which spans the membrane from the extra- to the intracellular side. A tethered ligand located between the extracellular loops has been proven and is composed of amino acids from both C-terminal ends of the LRRD and the hinge region.