title: [Domain structure and signal transduction mechanisms in the thyrotropin receptor].
abstract: The thyrotropin receptor is a single polypeptide (744 amino acids) consisting of two domains (N-terminal extracellular domain and C-terminal transmembrane/cytoplasmic region). The former (398 aa) contains six potential glycosylation sites, 11 cysteins and 9 leucine rich repeats and is very likely to be the major TSH binding site. On the other hand, the latter (346 aa) has a characteristic of G protein coupled receptors (seven transmembrane segments, 3 extracellular-and cyto-plasmic loops and a carboxyl terminal tail), contains potential phosphorylation sites (serine/threonine residues) for c-kinase and G-protein coupled receptor kinase and plays important roles in signal transduction and homologous desensitization. Experimentally-produced and naturally-occurring mutant receptors provide molecular mechanisms of receptor function.
authors.affiliation: First Department of Internal Medicine, Nagasaki University School of Medicine.
authors.forename: Y
authors.initials: Y
authors.lastname: Nagayama
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004247:DNA; D006801:Humans; D010766:Phosphorylation; D011989:Receptors, Thyrotropin / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D015398:Signal Transduction
chemical_list: D011989:Receptors, Thyrotropin; D004247:DNA