ArticleAuto- immunity highlights2017
Structure and activation of the TSH receptor transmembrane domain.
Article in Auto- immunity highlights, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
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- Structure of full-length TSH receptor in complex with antibody K1-70™.Journal of molecular endocrinology · 2023Article
- Structural basis of signaling regulation of the human melanocortin-2 receptor by MRAP1.Cell research · 2023Article
- 2021 update on thyroid-associated ophthalmopathy.Journal of endocrinological investigation · 2022Review
- Evaluation of analytic and clinical performance of two immunoassays for detecting thyroid-stimulating receptor antibody in the diagnosis of Graves' disease.Journal of clinical laboratory analysis · 2021Article
- Cryo-EM: A new dawn in thyroid biology.Molecular and cellular endocrinology · 2021Review
- Implications of an Improved Model of the TSH Receptor Transmembrane Domain (TSHR-TMD-TRIO).Endocrinology · 2021Article
- The Role of Hormones and Trophic Factors as Components of Preservation Solutions in Protection of Renal Function before Transplantation: A Review of the Literature.Molecules (Basel, Switzerland) · 2020Review
- New Thieno-[2,3-d]pyrimidine-Based Functional Antagonist for the Receptor of Thyroid Stimulating Hormone.Doklady. Biochemistry and biophysics · 2020Article
- Receptor autoimmunity: diagnostic and therapeutic implications.Auto- immunity highlights · 2020Review
- Structural Biology Helps Interpret Variants of Uncertain Significance in Genes Causing Endocrine and Metabolic Disorders.Journal of the Endocrine Society · 2018Article
- Structural-Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at Work.Frontiers in endocrinology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeThe thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves' disease. The TSHR is composed of: a leucine-rich repeat domain (LRD), a hinge region or cleavage domain (CD) and a transmembrane domain (TMD). The binding arrangements between the TSHR LRD and the thyroid-stimulating autoantibody M22 or TSH have become available from the crystal structure of the TSHR LRD-M22 complex and a comparative model of the TSHR LRD in complex with TSH, respectively. However, the mechanism by which the TMD of the TSHR and the other glycoprotein hormone receptors (GPHRs) becomes activated is unknown.
methodsWe have generated comparative models of the structures of the inactive (TMD_In) and active (TMD_Ac) conformations of the TSHR, follicle-stimulating hormone receptor (FSHR) and luteinizing hormone receptor (LHR) TMDs. The structures of TMD_Ac and TMD_In were obtained using class A GPCR crystal structures for which fully active and inactive conformations were available.
resultsMost conserved motifs observed in GPCR TMDs are also observed in the amino acid sequences of GPHR TMDs. Furthermore, most GPCR TMD conserved helix distortions are observed in our models of the structures of GPHR TMDs. Analysis of these structures has allowed us to propose a mechanism for activation of GPHR TMDs.
conclusionsInsight into the mechanism of activation of the TSHR by both TSH and TSHR autoantibodies is likely to be useful in the development of new treatments for Graves' disease.
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