THYROXINE PROTEIN INTERACTIONS

甲状腺素蛋白相互作用

• 批准号: 3876401
• 负责人: J ROBBINS
• 金额: --
• 依托单位: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3876401
• 关键词: apolipoproteins; binding proteins; chemical binding; conformation; fibroblasts; high density lipoproteins; human tissue; low density lipoprotein; monoclonal antibody; receptor; receptor mediated endocytosis; thyroid hormone binding protein; thyroid hormones; thyroxine; triiodothyronine

We previously demonstrated that high density lipoproteins (HDL) bind T4 in human plasma through a single binding site on apoA-I and that low density lipoproteins (LDL) bind T4 through 3 binding sites on apoB-100. By photoaffinity labeling with [(125)I]T4 and its inhibition by monoclonal antibodies to the apolipoproteins, we have investigated the location of the T4 binding sites. In apoA-I, the T4 site is in the N-terminal third of the molecule. In apoB-100, the T-4 sites are outside the LDL receptor binding domain and are located in the molecular domains designated as apoB-26, apoB-44 and apoB-30. Conformational changes due to interaction with lipids appear to result in altered patterns of monoclonal antibody inhibition.

我们以前证明，高密度脂蛋白（HDL）结合T4， 人血浆通过apoA-I上单个结合位点和最低密度 脂蛋白（LDL）通过apoB-100上的3个结合位点结合T4。通过 [（125）I] T_4光亲和标记及其单克隆抗体的抑制作用 载脂蛋白的抗体，我们已经研究了载脂蛋白的位置。 T4结合位点。在apoA-I中，T4位点位于apoA-I的N-末端三分之一， 分子。在apoB-100中，T-4位点在LDL受体结合之外 结构域并且位于被指定为apoB-26的分子结构域中， apoB-44和apoB-30。与脂质相互作用引起的构象变化 似乎导致单克隆抗体抑制模式的改变。