Table of Contents
Journal of Amino Acids
Volume 2011, Article ID 812540, 7 pages
Review Article

The Dynamic Structure of the Estrogen Receptor

1Department of Basic Sciences, The Commonwealth Medical College, Scranton, PA 18510, USA
2Section of Endocrinology, Boston University School of Medicine, Boston, MA 02118, USA
3Medical Genetics Institute, Cedars-Sinai Medical Center, Los Angeles, CA 90048, USA
4Division of Endocrinology and Metabolism, Charles Drew University of Medicine and Science, Los Angeles, CA 90059, USA

Received 1 April 2011; Accepted 6 June 2011

Academic Editor: Faizan Ahmad

Copyright © 2011 Raj Kumar et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.