Function of Estrogen Receptor Tryosine Phosphorylation
Abstract
The human estrogen receptor (hER), is the in vivo target of the female sex hormone estrogen. It is also the therapeutic target of various antiestrogens used during hormonal treatment in the battle of breast cancer. The purpose of this research is to exploit the known structure-function relations of the hER protein to develop novel approaches at regulating hER function. The scope of this research involves the study of novel inhibitory peptides which appear to block hER dimerization. Our latest findings have compelled a revision of our earlier hypothesis regarding the phosphotyrosine mediated dimerization of the hER. During the last year we have made significant progress in understanding the role of tyrosine 537 in hER function and in evaluating phosphopeptides as hER inhibitors. We now show that the phosphotyrosyl peptide, derived from the C-terminal helix 12 of the hER ligand binding domain (LBD), inhibits hER DNA binding through a LBD-dependent mechanism. The sequence specificity of this peptide is also further characterized.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 1998
- Accession Number
- ADB241069
Entities
People
- Matthew R. Yudt
Organizations
- University of Rochester