The Structural Studies Of The Interaction Between Nur77 And Dax1

Nuclear receptors play important roles in the cellular processes.There are 48 human nuclear receptors identified up to date,which can be classified as transcription factors and cotranscription factors.This thesis focuses on two nuclear receptors,one is a transcription factor and the other is a cotranscription factor.Nur77 is an orphan nuclear recptor,as its physiological ligand has not been identified.Nur77 is a transcription factor and involved in cancer cells' mitosis.Down-regulating Nur77 by RNAi will cause cancers cell's proliferation.Nur77 can directly actived cytokine P45017 promoter for the production of many steroids including androgen.Androgen and Nur77 itself prompt the growth of prostate cancer.It is possible to impede the cancer growth by repressing the Nur77's transcriptional activity.Dax1 is another orphan nuclear receptor that can directly bind to Nur77 to regulate its transcriptional activity.In this work,we identified a Dax1's sequence that interacted with Nur77,crystallized the complex between Nur77 and the Dax1 peptide,and made an attempt to sovle the structure by X ray crystallography,which set a foundation for future studies.