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Crystal structure of a beta-catenin/Tcf complex.

The Wnt signaling pathway plays critical roles in embryonic development and tumorigenesis. Stimulation of the Wnt pathway results in the accumulation of a nuclear beta-catenin/Tcf complex, activating Wnt target genes. A crystal structure of beta-catenin bound to the beta-catenin binding domain of Tcf3 (Tcf3-CBD) has been determined. The Tcf3-CBD forms an elongated structure with three binding modules that runs antiparallel to beta-catenin along the positively charged groove formed by the armadillo repeats. Structure-based mutagenesis defines three sites in beta-catenin that are critical for binding the Tcf3-CBD and are differentially involved in binding APC, cadherin, and Axin. The structural and mutagenesis data reveal a potential target for molecular drug design studies.

Pubmed ID: 11136974

Authors

  • Graham TA
  • Weaver C
  • Mao F
  • Kimelman D
  • Xu W

Journal

Cell

Publication Data

December 8, 2000

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM07270
  • Agency: NICHD NIH HHS, Id: HD07183
  • Agency: NICHD NIH HHS, Id: HD27262

Mesh Terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Axin Protein
  • Cadherins
  • Crystallography, X-Ray
  • Cytoskeletal Proteins
  • HMGB Proteins
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Precipitin Tests
  • Protein Binding
  • Protein Conformation
  • Proteins
  • Repressor Proteins
  • Sequence Alignment
  • Signal Transduction
  • TCF Transcription Factors
  • Trans-Activators
  • Transcription Factor 7-Like 1 Protein
  • Transcription Factors
  • Xenopus
  • Xenopus Proteins
  • beta Catenin