Prokaryotic expression of homo androgen receptor DNA binding domain and co-crystallization with androgen response element

Abstract:

Obtained a highresolution complex crystal structure of the androgen receptor (AR) and its response element (ARE) could provide a theoretical basis for drug target design for the treatment of prostate cancer. In this study, a prokaryotic expression vector of AR-DBD was constructed, and the protein was inducted to expression at 16 ℃ with 0.5 mmol/L IPTG for 24 h. In order to purify AR-DBD protein easily, the protein purification conditions were optimized by binding to ARE oligonucleic acids. Finally, we obtained the proteinnucleic acid complex crystal that exhibited short rodlike threedimensional structures with clear crystal edges. The proteinnucleotide complex crystals prepared in this study can be used for Xray diffraction analysis directly.