Crystal structure of a beta-catenin/Tcf complex

Article Abstract:

Analysis of the crystal structure of beta-catenin and its binding domain (Tcf3 Tcf3-CBD) reveals three binding modules running antiparallel to beta-catenin. Data also show three sites in beta-catenin involved in the binding of Apc, Cadherin, and axin through Tcf3-CBD.

United States, Statistical Data Included, Physiological aspects, Cellular signal transduction, Cell adhesion

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Crystal structure of a beta-catenin/Axin complex suggests a mechanism for the beta-catenin destruction complex

Article Abstract:

The crystal structure of a complex between beta-catenin and the beta-catenin-binding domain of Axin is determined. A key function of Adenomatous Polyposis Coli (APC) protein in the beta-catenin destruction complex is to remove phosphorylated b-catenin product from the active site.

Science & research, Phosphorylation, Genetic research, Polyposis, Familial, Familial polyposis, Properties, Structure

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Crystal structure of a paired domain-DNA complex at 2.5 angstrom resolution reveals structural basis for Pax developmental mutations

Article Abstract:

A 25 angstrom resolution crystal structure of the cocrystal that has the paired domain from the paired (prd) protein of Drosophila and a 15 bp optimized binding site helps study the function of paired domain in DNA recognition and gene regulation. Each of the C- and N-terminal subdomains has the recombinase and the homeodomain-like helical region. Numerous DNA contacts occur at the N-terminal domain through a new beta-turn motif, which binds in the minor groove, and a helix-turn-helix unit. prd binding does not require the C-terminal domains, which do not associate with the optimized binding site.

Proteins, Drosophila, Protein structure

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