Abstract
The estrogen receptor (ER) mediates most of the biological effects of estrogens at the level of gene regulation by interacting through its site-specific DNA and with other coregulatory proteins. In recent years, new information regarding the dynamic structural nature of ER has emerged. The physiological effects of estrogen are manifested through ER's two isoforms, ERα and ERβ. These two isoforms (ERα and ERβ) display distinct regions of sequence homology. The three-dimensional structures of the DNA-binding domain (DBD) and ligand-binding domain (LBD) have been solved, whereas no three-dimensional natively folded structure for the ER N-terminal domain (NTD) is available to date. However, insights about the structural and functional correlations regarding the ER NTD have recently emerged. In this paper, we discuss the knowledge about the structural characteristics of the ER in general and how the structural features of the two isoforms differ, and its subsequent role in gene regulation.
Highlights
The estrogen receptor (ER) is a ligand-inducible intracellular transcription factor that mediates most of the biological effects of estrogens at the level of gene regulation [1,2,3]
We focus on the two isoforms of human ER (ERα (NR3A1) and ERβ (NR3A2)), encoded by two different genes
Recent observations have led to the conclusion that in cells, ER and several other nuclear hormone receptor (NHR) behave very dynamically such that their kinetic behavior in cells allows them to rapidly interact with various coregulatory proteins, and with chromatin and DNA [80]
Summary
The estrogen receptor (ER) is a ligand-inducible intracellular transcription factor that mediates most of the biological effects of estrogens at the level of gene regulation [1,2,3]. Two activation function (AF) domains, AF1 and AF2, located within the NTD and LBD, respectively, are responsible for regulating the transcriptional activity of ER [12] (Figure 1(a)). We focus on the two isoforms of human ER (ERα (NR3A1) and ERβ (NR3A2)), encoded by two different genes. Both have been cloned and characterized [18]. The three-dimensional structures of the independently expressed DBD and LBD have been solved and show overall folds that represent globular proteins with natively ordered conformations [13, 23,24,25]. We discuss the knowledge about the structural characteristics of the ER and its role in gene regulation
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