3F5C

Structure of Dax-1:LRH-1 complex

Summary for 3F5C

• Entry DOI: 10.2210/pdb3f5c/pdb
• Descriptor: Nuclear receptor subfamily 5 group A member 2, Nuclear receptor subfamily 0 group B member 1 (2 entities in total)
• Functional Keywords: nuclear receptor, transcriptional corepressor, regulatory complex, dna-binding, lipid-binding, metal-binding, nucleus, receptor, transcription, transcription regulation, zinc, zinc-finger, cytoplasm, repressor
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 3
• Total formula weight: 89481.98

Authors

Fletterick, R.J.,Sablin, E.P. (deposition date: 2008-11-03, release date: 2008-12-23, Last modification date: 2023-09-06)

Primary citation

Sablin, E.P.,Woods, A.,Krylova, I.N.,Hwang, P.,Ingraham, H.A.,Fletterick, R.J.
The structure of corepressor Dax-1 bound to its target nuclear receptor LRH-1.
Proc.Natl.Acad.Sci.USA, 105:18390-18395, 2008

PubMed Abstract: The Dax-1 protein is an enigmatic nuclear receptor that lacks an expected DNA binding domain, yet functions as a potent corepressor of nuclear receptors. Here we report the structure of Dax-1 bound to one of its targets, liver receptor homolog 1 (LRH-1). Unexpectedly, Dax-1 binds to LRH-1 using a new module, a repressor helix built from a family conserved sequence motif, PCFXXLP. Mutations in this repressor helix that are linked with human endocrine disorders dissociate the complex and attenuate Dax-1 function. The structure of the Dax-1:LRH-1 complex provides the molecular mechanism for the function of Dax-1 as a potent transcriptional repressor.

PubMed: 19015525
DOI: 10.1073/pnas.0808936105

Experimental method

X-RAY DIFFRACTION (3 Å)