Structural highlights
Publication Abstract from PubMed
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.
The structure of corepressor Dax-1 bound to its target nuclear receptor LRH-1.,Sablin EP, Woods A, Krylova IN, Hwang P, Ingraham HA, Fletterick RJ Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18390-5. Epub 2008 Nov 17. PMID:19015525[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sablin EP, Woods A, Krylova IN, Hwang P, Ingraham HA, Fletterick RJ. The structure of corepressor Dax-1 bound to its target nuclear receptor LRH-1. Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18390-5. Epub 2008 Nov 17. PMID:19015525 doi:http://dx.doi.org/0808936105
