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Structure of a human Tcf4-beta-catenin complex.

The multifunctional protein beta-catenin is important for cell adhesion, because it binds cadherins, and the Wnt signal transduction pathway, where it interacts with the Adenomatous polyposis coli (APC) protein and TCF/Lef family transcription factors. Mutations in APC or in beta-catenin are estimated to trigger formation of over 90% of all colon cancers. In colonic epithelia, these mutations produce elevated levels of Tcf4-beta-catenin, which stimulates a transcriptional response that initiates polyp formation and eventually malignant growth. Thus, disruption of the Tcf4-beta-catenin interaction may be an attractive goal for therapeutic intervention. Here we describe the crystal structure of a human Tcf4-beta-catenin complex and compare it with recent structures of beta-catenin in complex with Xenopus Tcf3 (XTcf3) and mammalian E-cadherin. The structure reveals anticipated similarities with the closely related XTcf3 complex but unexpectedly lacks one component observed in the XTcf3 structure.

Pubmed ID: 11713476


  • Poy F
  • Lepourcelet M
  • Shivdasani RA
  • Eck MJ


Nature structural biology

Publication Data

December 27, 2001

Associated Grants


Mesh Terms

  • Animals
  • Binding Sites
  • Cadherins
  • Cell Line
  • Crystallography, X-Ray
  • Cytoskeletal Proteins
  • Drug Design
  • Genes, Reporter
  • HMGB Proteins
  • Humans
  • Hydrogen Bonding
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Repetitive Sequences, Amino Acid
  • Static Electricity
  • TCF Transcription Factors
  • Trans-Activators
  • Transcription Factor 7-Like 1 Protein
  • Transcription Factor 7-Like 2 Protein
  • Transcription Factors
  • Transfection
  • Xenopus Proteins
  • beta Catenin