Weigel N L, Beck C A, Estes P A, Prendergast P, Altmann M, Christensen K, Edwards D P
Baylor College of Medicine, Cell Biology Department, Houston, Texas 77030.
Mol Endocrinol. 1992 Oct;6(10):1585-97. doi: 10.1210/mend.6.10.1448113.
We have prepared a monoclonal antibody, C-262, to a synthetic peptide that contains the carboxy-terminal 14 amino acids from progesterone receptors (PR). This sequence is 100% conserved in all species of PRs that have been cloned to date, suggesting that this antibody will recognize all mammalian and avian PR. The C-262 antibody recognizes both native and denatured forms of the receptor. However, it does not recognize PR when they are bound to the hormone agonists progesterone or R5020. Surprisingly the antibody does recognize PR when they are bound to the steroid antagonist RU486. This suggests that progestin agonists induce a conformational change in the receptor that occludes the C-262 epitope in the carboxyl-terminus, whereas unliganded receptors and receptors bound with RU486 assume distinct conformations that leaves the C-terminal tail accessible to the C-262 antibody.
我们制备了一种针对合成肽的单克隆抗体C-262，该合成肽包含孕激素受体（PR）羧基末端的14个氨基酸。在迄今已克隆的所有PR物种中，该序列100%保守，这表明该抗体将识别所有哺乳动物和禽类的PR。C-262抗体可识别受体的天然形式和变性形式。然而，当PR与激素激动剂孕酮或R5020结合时，它无法识别PR。令人惊讶的是，当PR与类固醇拮抗剂RU486结合时，该抗体确实能识别PR。这表明孕激素激动剂会诱导受体发生构象变化，从而遮蔽羧基末端的C-262表位，而未结合配体的受体以及与RU486结合的受体呈现出不同的构象，使得C-末端尾巴能够被C-262抗体识别。
