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
  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray
  • Humans
  • Ligands
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments/chemistry
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Zebrafish
  • beta Catenin/chemistry*
  • beta Catenin/metabolism
PubMed
18334222 Full text @ Structure
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
Figures
Show all Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping