CONFORMATIONAL-CHANGES IN CHICKEN THYROID-HORMONE RECEPTOR-ALPHA-1 INDUCED BY BINDING TO LIGAND OR TO DNA

被引：64

作者：

TONEY, JH

WU, L

SUMMERFIELD, AE

SANYAL, G

FORMAN, BM

ZHU, JB

SAMUELS, HH

机构：

[1] MERCK SHARP & DOHME LTD,PHARMACEUT RES,W POINT,PA 19486

[2] NYU MED CTR,DEPT MED,DIV MOLEC ENDOCRINOL,NEW YORK,NY 10016

[3] NYU MED CTR,DEPT PHARMACOL,NEW YORK,NY 10016

来源：

BIOCHEMISTRY | 1993年 / 32卷 / 01期

关键词：

D O I：

10.1021/bi00052a001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A classic model of steroid/thyroid hormone receptor activation postulates that a conformational change or ''transformation'' occurs upon ligand binding as a first step toward regulation of gene transcription. In order to test this model, physical studies have been carried out using purified full-length chicken thyroid hormone receptor alpha1 (cT3R-alpha1) expressed in Escherichia coli. Circular dichroism spectroscopic studies reveal that cT3R-alpha1 adopts a different conformation upon specific binding to a cognate ligand triiodothyroacetic acid as well as to a thyroid hormone response element, an idealized inverted repeat AGGTCA TGACCT. These results suggest that cT3R-alpha1 may adopt distinct conformations whether free or bound to ligand or to DNA. These states may reflect the changes in the conformation of steroid/thyroid hormone receptors in the signal transduction pathway.

引用

页码：2 / 6

页数：5

共 27 条

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