Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 1, Pages 143-148Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1117036108
Keywords
crystal structure; crystallography; protein-protein interaction
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Funding
- National Institutes of Health [R01 DK078075, R21 DK084504, DK51281, DK41482]
- Uehara Memorial Foundation (Tokyo, Japan)
- Department of Biophysics and Biochemistry, University of California, San Francisco (UCSF)
- UCSF
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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 angstrom 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.
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