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Updated: Aug 6, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
Identification of a highly conserved domain in the androgen receptor that suppresses the DNA-binding domain-DNA
Guo-Zhen Liu1, Hua Wang, Zhengxin Wang
1Department of Cancer Biology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030-4009, USA.
Abstract:
The androgen receptor (AR) is a ligand-regulated and sequence-specific transcription factor that activates or represses expression of target genes. Here, we show that the N terminus of AR contains an inhibitory domain located in an 81-amino acid segment lying upstream of the DNA-binding domain (DBD). The inhibitory domain interacted directly with DBD and repressed DBD binding to the androgen response element. Mutations of the conserved amino acid residues (K520E and R538E) within the inhibitory domain decreased its inhibiting ability in vitro and increased AR trans-activation in vivo. These data demonstrate the existence of a novel inhibitory domain in the N-terminal part of AR, which might play important roles in the regulation of AR trans-activation.
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