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Crystal structure of a beta-catenin/Tcf complex.

Cell | Dec 8, 2000

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 RIS Download

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

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