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1th1

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[[Image:1th1.gif|left|200px]]
[[Image:1th1.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1th1 |SIZE=350|CAPTION= <scene name='initialview01'>1th1</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1th1", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= CTNNB1, CTNNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), APC, DP2.5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1th1| PDB=1th1 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1th1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1th1 OCA], [http://www.ebi.ac.uk/pdbsum/1th1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1th1 RCSB]</span>
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'''Beta-catenin in complex with a phosphorylated APC 20aa repeat fragment'''
'''Beta-catenin in complex with a phosphorylated APC 20aa repeat fragment'''
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[[Category: Xing, Y.]]
[[Category: Xing, Y.]]
[[Category: Xu, W.]]
[[Category: Xu, W.]]
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[[Category: protein-protein complex]]
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[[Category: Protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:56:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:55 2008''
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Revision as of 06:56, 3 May 2008

Image:1th1.gif

Template:STRUCTURE 1th1

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


Overview

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.

About this Structure

1TH1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a beta-catenin/APC complex reveals a critical role for APC phosphorylation in APC function., Xing Y, Clements WK, Le Trong I, Hinds TR, Stenkamp R, Kimelman D, Xu W, Mol Cell. 2004 Aug 27;15(4):523-33. PMID:15327769 Page seeded by OCA on Sat May 3 09:56:19 2008

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