3TX7

Crystal structure of LRH-1/beta-catenin complex

Summary for 3TX7

• Entry DOI: 10.2210/pdb3tx7/pdb
• Descriptor: Catenin beta-1, Nuclear receptor subfamily 5 group A member 2, (2S)-3-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-[(6E)-HEXADEC-6-ENOYLOXY]PROPYL (8E)-OCTADEC-8-ENOATE (3 entities in total)
• Functional Keywords: lrh-1, beta-catenin, armadillo repeat, nuclear receptor ligand binding domain, protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P35222; Nucleus (Probable): O00482
• Total number of polymer chains: 2
• Total formula weight: 98272.31

Authors

Yumoto, F.,Fletterick, R. (deposition date: 2011-09-22, release date: 2011-12-14, Last modification date: 2023-09-13)

Primary citation

Yumoto, F.,Nguyen, P.,Sablin, E.P.,Baxter, J.D.,Webb, P.,Fletterick, R.J.
Structural basis of coactivation of liver receptor homolog-1 by beta-catenin.
Proc.Natl.Acad.Sci.USA, 109:143-148, 2012

PubMed Abstract: We report the three-dimensional structure of a β-catenin armadillo repeat in complex with the liver receptor homolog-1 (LRH-1) ligand binding domain at 2.8 Å resolution as the first structure of β-catenin in complex with any nuclear receptor. The surface of β-catenin that binds LRH-1 partly overlaps defined contact sites for peptide segments of β-catenin partners, including T-cell factor-4. The surface of LRH-1 that engages β-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/β-catenin interface reveals that they are essential for stable interactions between these proteins in solution. The LRH-1 binding site in β-catenin is also required for association with androgen receptor, providing evidence that the observed LRH-1/β-catenin interaction may be prototypic.

PubMed: 22187462
DOI: 10.1073/pnas.1117036108

Experimental method

X-RAY DIFFRACTION (2.76 Å)