PUBLICATION
Crystal Structure of a Full-Length beta-Catenin
- Authors
- Xing, Y., Takemaru, K., Liu, J., Berndt, J.D., Zheng, J.J., Moon, R.T., and Xu, W.
- ID
- ZDB-PUB-080326-3
- Date
- 2008
- Source
- Structure (London, England : 1993) 16(3): 478-487 (Journal)
- Registered Authors
- Berndt, Jason, Moon, Randall T.
- Keywords
- none
- MeSH Terms
-
- Crystallography, X-Ray
- Models, Molecular
- Peptide Fragments/chemistry
- Amino Acid Sequence
- Animals
- Molecular Sequence Data
- Models, Biological
- Protein Binding
- Zebrafish
- Nuclear Magnetic Resonance, Biomolecular
- beta Catenin/chemistry*
- beta Catenin/metabolism
- Protein Structure, Tertiary
- Sequence Homology, Amino Acid
- Humans
- Ligands
- PubMed
- 18334222 Full text @ Structure
Citation
Xing, Y., Takemaru, K., Liu, J., Berndt, J.D., Zheng, J.J., Moon, R.T., and Xu, W. (2008) Crystal Structure of a Full-Length beta-Catenin. Structure (London, England : 1993). 16(3):478-487.
Abstract
beta-catenin plays essential roles in cell adhesion and Wnt signaling, while deregulation of beta-catenin is associated with multiple diseases including cancers. Here, we report the crystal structures of full-length zebrafish beta-catenin and a human beta-catenin fragment that contains both the armadillo repeat and the C-terminal domains. Our structures reveal that the N-terminal region of the C-terminal domain, a key component of the C-terminal transactivation domain, forms a long alpha helix that packs on the C-terminal end of the armadillo repeat domain, and thus forms part of the beta-catenin superhelical core. The existence of this helix redefines our view of interactions of beta-catenin with some of its critical partners, including ICAT and Chibby, which may form extensive interactions with this C-terminal domain alpha helix. Our crystallographic and NMR studies also suggest that the unstructured N-terminal and C-terminal tails interact with the ordered armadillo repeat domain in a dynamic and variable manner.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping