THE HUMAN ESTROGEN-RECEPTOR HORMONE-BINDING DOMAIN DIMERIZES INDEPENDENTLY OF LIGAND ACTIVATION

被引：26

作者：

SALOMONSSON, M

HAGGBLAD, J

OMALLEY, BW

SITBON, GM

机构：

[1] KARO BIO AB,S-14104 HUDDINGE,SWEDEN

[2] BAYLOR COLL MED,DEPT CELL BIOL,HOUSTON,TX 77030

来源：

JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY | 1994年 / 48卷 / 5-6期

关键词：

D O I：

10.1016/0960-0760(94)90192-9

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：

High level expression of biochemically active human estrogen receptor hormone binding domain (hER-HBD) was achieved using a Saccharomyces cerevisae expression system. Using dissociation kinetic analysis, density gradient centrifugation and cross-linking studies, a spontaneous dimerization activity of hER-HBD independent of the presence of the DNA binding domain, ligand, and of elevated temperature is demonstrated.

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页码：447 / 452

页数：6

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