| First Author | Huber AH | Year | 2001 |
| Journal | Cell | Volume | 105 |
| Issue | 3 | Pages | 391-402 |
| PubMed ID | 11348595 | Mgi Jnum | J:182415 |
| Mgi Id | MGI:5315371 | Doi | 10.1016/s0092-8674(01)00330-0 |
| Citation | Huber AH, et al. (2001) The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin. Cell 105(3):391-402 |
| abstractText | As a component of adherens junctions and the Wnt signaling pathway, beta-catenin binds cadherins, Tcf family transcription factors, and the tumor suppressor APC. We have determined the crystal structures of both unphosphorylated and phosphorylated E-cadherin cytoplasmic domain complexed with the arm repeat region of beta-catenin. The interaction spans all 12 arm repeats, and features quasi-independent binding regions that include helices which interact with both ends of the arm repeat domain and an extended stretch of 14 residues which closely resembles a portion of XTcf-3. Phosphorylation of E-cadherin results in interactions with a hydrophobic patch of beta-catenin that mimics the binding of an amphipathic XTcf-3 helix. APC contains sequences homologous to the phosphorylated region of cadherin, and is likely to bind similarly. |
