Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3
The structure was published by Ha, N.-C., Tonozuka, T., Stamos, J.L., Choi, H.J., and Weis, W.I., in 2004 in a paper entitled "Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2004.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 3 biomacromolecules, namely Beta-catenin, Beta-catenin-interacting protein 1, and Adenomatous polyposis coli protein.
The molecule most likely forms heterotrimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 3 unique UniProt proteins: