Brtko J, Knopp J
Ustavu experimentálnej endokrinológie CFV SAV v Bratislave.
Bratisl Lek Listy. 1990 Mar;91(3):167-71.
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.
本文描述了非组蛋白蛋白质化学修饰诱导甲状腺激素受体结合特性的调节。在核水平上，对甲状腺激素的生物学反应由激素-受体复合物的形成决定，该复合物作为激素作用的起始因子。常用生化分离方法的结合仅能实现甲状腺激素受体的部分纯化。c-erb-A基因的产物携带代表甲状腺激素受体的序列。目前，受体分子上甲状腺激素特异性结合位点的结构和确切氨基酸序列均未知。已发现具有生物活性的甲状腺激素-受体复合物的形成需要保留3,5,3'-三碘甲状腺原氨酸受体组氨酸残基的19个亲核咪唑基团中的至少一个。
