ASSOCIATION OF HEAT-SHOCK PROTEIN-90 WITH THE 16KDA STEROID BINDING CORE FRAGMENT OF RAT GLUCOCORTICOID RECEPTORS

被引：27

作者：

CHAKRABORTI, PK ^{[1
]}

SIMONS, SS ^{[1
]}

机构：

[1] NIDDK,STEROID HORMONES SECT,BLDG 8,RM B2A07,BETHESDA,MD 20892

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 176卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)90433-8

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：

We have recently described a 16 kDa steroid binding core (Thr537-Arg673) of the rat glucocorticoid receptor [Simons et al. (1989) J. Biol. Chem. 264, 14493-14497]. Sedimentation analysis and size exclusion and anion exchange chromatography now suggest that other proteins are associated with the 16 kDa receptor, just as has been seen for the intact 98 kDa receptor. The 16 kDa fragment was also immunoprecipitable with anti-heat shock protein 90 (hsp90) antibody. These results argue that hsp90 binds to the 16 kDa core fragment and directly position the site of hsp90 association between Thr537 and Arg673 of the rat glucocorticoid receptor. © 1991.

引用

页码：1338 / 1344

页数：7

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