1t08

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[[Image:1t08.gif|left|200px]]
[[Image:1t08.gif|left|200px]]
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{{Structure
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|PDB= 1t08 |SIZE=350|CAPTION= <scene name='initialview01'>1t08</scene>, resolution 2.10&Aring;
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The line below this paragraph, containing "STRUCTURE_1t08", 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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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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]), CTNNBIP1,ICAT ([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_1t08| PDB=1t08 | 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=1t08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t08 OCA], [http://www.ebi.ac.uk/pdbsum/1t08 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t08 RCSB]</span>
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'''Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3'''
'''Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3'''
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[[Category: Weis, W I.]]
[[Category: Weis, W I.]]
[[Category: 20mer repeat]]
[[Category: 20mer repeat]]
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[[Category: apc]]
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[[Category: Apc]]
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[[Category: beta-catenin]]
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[[Category: Beta-catenin]]
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[[Category: wnt signal]]
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[[Category: Wnt signal]]
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[[Category: wnt signaling]]
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[[Category: Wnt signaling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:20:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:20 2008''
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Revision as of 06:20, 3 May 2008

Image:1t08.gif

Template:STRUCTURE 1t08

Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3


Overview

The transcriptional coactivator beta-catenin mediates Wnt growth factor signaling. In the absence of a Wnt signal, casein kinase 1 (CK1) and glycogen synthase kinase-3beta (GSK-3beta) phosphorylate cytosolic beta-catenin, thereby flagging it for recognition and destruction by the ubiquitin/proteosome machinery. Phosphorylation occurs in a multiprotein complex that includes the kinases, beta-catenin, axin, and the Adenomatous Polyposis Coli (APC) protein. The role of APC in this process is poorly understood. CK1epsilon and GSK-3beta phosphorylate APC, which increases its affinity for beta-catenin. Crystal structures of phosphorylated and nonphosphorylated APC bound to beta-catenin reveal a phosphorylation-dependent binding motif generated by mutual priming of CK1 and GSK-3beta substrate sequences. Axin is shown to act as a scaffold for substrate phosphorylation by these kinases. Phosphorylated APC and axin bind to the same surface of, and compete directly for, beta-catenin. The structural and biochemical data suggest a novel model for how APC functions in beta-catenin degradation.

About this Structure

1T08 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation., Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI, Mol Cell. 2004 Aug 27;15(4):511-21. PMID:15327768 Page seeded by OCA on Sat May 3 09:20:30 2008

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