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

被引：15

作者：

Luck, LA ^{[1
]}

Barse, JL ^{[1
]}

Luck, AM ^{[1
]}

Peck, CH ^{[1
]}

机构：

[1] Clarkson Univ, Dept Biol & Chem, Potsdam, NY 13699 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 270卷 / 03期

关键词：

F-19; NMR; estrogen receptor; estradiol; conformational change; hormone binding domain; nuclear receptors;

D O I：

10.1006/bbrc.2000.2526

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：

The F-19 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 farm. This study shows the applicability of F-19 NMR to study conformational change in large protein systems. (C) 2000 Academic Press.

引用

收藏

页码：988 / 991

页数：4

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