[Modulation of the binding characteristics of thyroid hormone receptors by the chemical modification of non-histone nuclear proteins].
Modulation of binding characteristics of thyroid hormone receptors induced by chemical modification of nonhistone proteins is described. At nuclear level, the biological response to thyroid hormones is determined by the formation of hormone-receptor complexes which act as the initiation factor of hormone action. The combination of common biochemical separation methods allows only partial purification of the thyroid hormone receptors. The product of the c-erb-A genes carries the sequence representing the thyroid hormone receptor. At present neither the structure nor the exact amino acid sequence of the specific binding site for the thyroid hormone at the receptor molecule is known. The formation of the biologically active thyroid hormone-receptor complex was found to require the preservation of at least one of the 19 nucleophilic imidazole groups of the histidyl residues of the 3,5,3'-triidothyronine receptor.
Brtko
J
J
Ustavu experimentálnej endokrinológie CFV SAV v Bratislave.
Knopp
J
J
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone / Q000187:drug effects*; D008099:Liver / Q000378:metabolism; D051381:Rats; D011988:Receptors, Thyroid Hormone / Q000187:drug effects / Q000378:metabolism*; D014284:Triiodothyronine / Q000378:metabolism; D014302:Trinitrobenzenesulfonic Acid / Q000494:pharmacology
D002868:Chromosomal Proteins, Non-Histone; D011988:Receptors, Thyroid Hormone; D014284:Triiodothyronine; D014302:Trinitrobenzenesulfonic Acid
Modulácia väzbových charakteristík receptorov pre hormóny stítnej zl'azy chemickou modifikáciou nehistónových proteínov bunkových jadier.