WebThe 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. WebThe thyrotropin (TSH) receptor (TSHR) is a key protein in the control of thyroid function and a major thyroid autoantigen. Recently, molecular cloning of the receptor has been carried …
Autoantibody mimicry of hormone action at the thyrotropin receptor
WebThe protein encoded by this gene is a membrane protein and a major controller of thyroid cell metabolism. The encoded protein is a receptor for thyrothropin and thyrostimulin, and its activity is mediated by adenylate cyclase. Defects in this gene are a cause of several types of hyperthyroidism. Three transcript variants encoding different isoforms have been found … WebJan 1, 2024 · 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 … china city of america
Thyroid-stimulating hormone and thyroid-stimulating hormone
WebJan 27, 2009 · Crystal structure of the TSH receptor in complex with a thyroid-stimulating autoantibody. ... Gene Names: TSHR, LGR3: UniProt & NIH Common Fund Data … WebAlso, 5C9 and similar MAbs have considerable potential as drugs to inhibit TSHR stimulation by autoantibodies. Further, now the M22-TSHR structure is known at the atomic level, rational design of specific low-molecular-weight inhibitors of the TSHR-TSHR autoantibody interaction is feasible. WebJul 1, 2024 · TSHR was purified after detergent lysis of whole cells, followed by immobilised metal ion affinity chromatography (IMAC ) and FLAG immunoaffinity chromatography. Unlike most other Class A GPCRs, TSHR is sufficiently large for its structure to be determined by single-particle cryo-EM in the ligand-free state. china city oak park