ArticleJournal of molecular endocrinology2023
Structure of full-length TSH receptor in complex with antibody K1-70™.
Article in Journal of molecular endocrinology, 2023. 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, 13 citations in OpenAlex.
- TSH receptor autoantibodies - a personal experience.Thyroid research · 2026Review
- Conformational equilibria in the activation of cystine-knot hormone receptors.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Predicting Pathogenicity ofInternational journal of molecular sciences · 2026Article
- The thyrotropin receptor structure and interactions with autoantibodies.European thyroid journal · 2025Review
- Autoantibodies to the TSH Receptor-from discovery to understanding the mechanisms of action and to new therapeutics.Endocrine journal · 2025Review
- Expression, immunogenicity and clinical significance analysis of thyroid‑stimulating hormone receptor fusion proteins.Molecular medicine reports · 2025Article
- Expression of the Extracellular Domain of the Thyrotropin Receptor Based on mRNA Isolated from Thyroid Tissue and Whole Blood of Patients with Toxic Diffuse Goiter (Graves' Disease).Bulletin of experimental biology and medicine · 2025Article
- A Comprehensive Review of Thyroid Eye Disease Pathogenesis: From Immune Dysregulations to Novel Diagnostic and Therapeutic Approaches.International journal of molecular sciences · 2024Review
- The changing landscape of thyroid eye disease: current clinical advances and future outlook.Eye (London, England) · 2024Review
- Mechanisms of thyrotropin receptor-mediated phenotype variability deciphered by gene mutations and M453T-knockin model.JCI insight · 2024Article
- Allosteric Regulation of G-Protein-Coupled Receptors: From Diversity of Molecular Mechanisms to Multiple Allosteric Sites and Their Ligands.International journal of molecular sciences · 2023Review
- Receptor modulators associated with the hypothalamus -pituitary-thyroid axis.Frontiers in pharmacology · 2023Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Determination of the full-length thyroid-stimulating hormone receptor (TSHR) structure by cryo-electron microscopy (cryo-EM) is described. The TSHR complexed with human monoclonal TSHR autoantibody K1-70™ (a powerful inhibitor of TSH action) was detergent solubilised, purified to homogeneity and analysed by cryo-EM. The structure (global resolution 3.3 Å) is a monomer with all three domains visible: leucine-rich domain (LRD), hinge region (HR) and transmembrane domain (TMD). The TSHR extracellular domain (ECD, composed of the LRD and HR) is positioned on top of the TMD extracellular surface. Extensive interactions between the TMD and ECD are observed in the structure, and their analysis provides an explanation of the effects of various TSHR mutations on TSHR constitutive activity and on ligand-induced activation. K1-70™ is seen to be well clear of the lipid bilayer. However, superimposition of M22™ (a human monoclonal TSHR autoantibody which is a powerful stimulator of the TSHR) on the cryo-EM structure shows that it would clash with the bilayer unless the TSHR HR rotates upwards as part of the M22™ binding process. This rotation could have an important role in TSHR stimulation by M22™ and as such provides an explanation as to why K1-70™ blocks the binding of TSH and M22™ without activating the receptor itself.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.