First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
|3tx7, resolution 2.76Å ()|
|Gene:||CTNNB1, CTNNB, OK/SW-cl.35, PRO2286 (Homo sapiens), NR5A2, B1F, CPF, FTF (Homo sapiens)|
Crystal structure of LRH-1/beta-catenin complex
We report the three-dimensional structure of a beta-catenin armadillo repeat in complex with the liver receptor homolog-1 (LRH-1) ligand binding domain at 2.8 A resolution as the first structure of beta-catenin in complex with any nuclear receptor. The surface of beta-catenin that binds LRH-1 partly overlaps defined contact sites for peptide segments of beta-catenin partners, including T-cell factor-4. The surface of LRH-1 that engages beta-catenin is comprised of helices 1, 9, and 10 and is distinct from known interaction surfaces of LRH-1, including corepressor and coactivator binding sites. Targeted mutagenesis of amino acids forming both sides of the LRH-1/beta-catenin interface reveals that they are essential for stable interactions between these proteins in solution. The LRH-1 binding site in beta-catenin is also required for association with androgen receptor, providing evidence that the observed LRH-1/beta-catenin interaction may be prototypic.
Structural basis of coactivation of liver receptor homolog-1 by beta-catenin., Yumoto F, Nguyen P, Sablin EP, Baxter JD, Webb P, Fletterick RJ, Proc Natl Acad Sci U S A. 2011 Dec 20. PMID:22187462
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.