1th1: Difference between revisions

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[[Image:1th1.gif|left|200px]]
{{Seed}}
[[Image:1th1.png|left|200px]]


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{{STRUCTURE_1th1|  PDB=1th1  |  SCENE=  }}  
{{STRUCTURE_1th1|  PDB=1th1  |  SCENE=  }}  


'''Beta-catenin in complex with a phosphorylated APC 20aa repeat fragment'''
===Beta-catenin in complex with a phosphorylated APC 20aa repeat fragment===




==Overview==
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The tumor suppressor adenomatous polyposis coli (APC) plays a critical role in the turnover of cytosolic beta-catenin, the key effector of the canonical Wnt signaling pathway. APC contains seven 20 amino acid (20 aa) beta-catenin binding repeats that are required for beta-catenin turnover. We have determined the crystal structure of beta-catenin in complex with a phosphorylated APC fragment containing two 20 aa repeats. Surprisingly, one single phosphorylated 20 aa repeat, together with its flanking regions, covers the entire structural groove of beta-catenin and may thus compete for beta-catenin binding with all other beta-catenin armadillo repeat partners. Our biochemical studies show that phosphorylation of the APC 20 aa repeats increases the affinity of the repeats for beta-catenin by 300- to 500-fold and the phosphorylated 20 aa repeats prevent beta-catenin binding to Tcf. Our work suggests that the phosphorylation of the APC 20 aa repeats could be a critical switch for APC function.
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{{ABSTRACT_PUBMED_15327769}}


==About this Structure==
==About this Structure==
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[[Category: Xu, W.]]
[[Category: Xu, W.]]
[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]
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