Endocrine Abstracts

The first crystal structure of human androgen receptor (AR) homodimer will be presented. This structure allows for the structure-based rationalization of the largest number of disease-associated mutations described for the AR ligand binding domain (LBD), which have been involved in prostate cancer and androgen insensitivity syndromes. The conservation of essential residues involved in AR self-association in other oxosteroid receptors suggests a more common dimerization mechanism.

DOI:10.1530/endoabs.42.IL3

Biographical details: Eva Estébanez-Perpiñá obtained her degrees in Biochemistry and Psychology (Psychobiology) from the Autonomous University of Barcelona (UAB). She did her Ph.D Thesis under the supervision of the Nobel Laureate Prof. Robert Huber and Prof. Wolfram Bode at the Max-Planck-Institut fuer Biochemie in Martinsried (Germany), where she graduated in 2002. She joined in 2003 the lab of Prof. Robert J. Fletterick at the University California, San Francisco (UCSF) to study the structure-function relationships of human nuclear receptors such as the androgen and the thyroid receptors. She started her Group at the Institute of Biomedicine, University of Barcelona (IBUB) in 2009 and became Associate Professor in 2015.