通过（19）F核磁共振观察到的人类雌激素受体的构象变化。

Conformational changes in the human estrogen receptor observed by (19)F NMR.

作者信息

Luck L A, Barse J L, Luck A M, Peck C H

机构信息

Department of Chemistry and Biology, Clarkson University, Potsdam, New York 13699, USA.

出版信息

Biochem Biophys Res Commun. 2000 Apr 21;270(3):988-91. doi: 10.1006/bbrc.2000.2526.

DOI:10.1006/bbrc.2000.2526

PMID:10772938

Abstract

The (19)F NMR spectra of the 5F-Trp labeled glutathione-S-transferase fusion protein with residues 282-595 of the human estrogen receptor show that there is a distinct conformational change in the protein when estradiol is added to the unliganded protein. Our studies show the empty receptor to have more conformational flexibility than the liganded form. This study shows the applicability of (19)F NMR to study conformational change in large protein systems.

摘要

含有人类雌激素受体282 - 595位残基的5F - Trp标记的谷胱甘肽 - S - 转移酶融合蛋白的（19）F核磁共振谱表明，当向未结合配体的蛋白中加入雌二醇时，该蛋白会发生明显的构象变化。我们的研究表明，未结合配体的受体比结合配体的形式具有更大的构象灵活性。这项研究表明了（19）F核磁共振在研究大型蛋白质系统构象变化方面的适用性。