Inhibitors for Androgen Receptor Activation Surfaces

Abstract

Studies from this grant led to discovery of a new interaction site on the androgen receptor for binding proteins that regulate the function of the receptor. The protein binders have not been identified, but we showed that the site has the characteristics of functioning in repression. We used X-ray crystallography to discover the binding mode of four compounds that bind to this site. Their binding is accompanied by weakening the interaction of the androgen receptor with coactivators as shown by disorder or representative peptides that were well ordered before adding the compounds. Thus, atomic level imaging of these interactions fit with the notion that the site functions in repression, as suggested by analysis of mutations of amino acid residues found in humans in cell and biochemical assays. This work suggests that compounds may be designed to target this site and weaken activity of the androgen receptor. Such compounds could form a new class of chemical therapeutics for treatment of prostate cancer.

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Document Details

Document Type
Technical Report
Publication Date
Sep 01, 2007
Accession Number
ADA476782

Entities

People

  • Robert J. Fletterick

Organizations

  • University of San Francisco

Tags

DTIC Thesaurus Topics

  • Amines
  • Amino Acids
  • Androgen Receptors
  • Chemical Analysis
  • Chemical Reactions
  • Chemical Synthesis
  • Chemistry
  • Crystallography
  • Diseases And Disorders
  • Liquid Chromatography
  • Mass Spectrometry
  • Molecules
  • Organic Chemistry
  • Small Molecules
  • Therapy
  • X Rays
  • X-Ray Crystallography

Fields of Study

  • Biology

Readers

  • Materials Science and Engineering.
  • Molecular Genetics
  • Prostate Cancer Biology.