1v18

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{{STRUCTURE_1v18| PDB=1v18 | SCENE= }}
{{STRUCTURE_1v18| PDB=1v18 | SCENE= }}
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'''THE CRYSTAL STRUCTURE OF BETA-CATENIN ARMADILLO REPEAT COMPLEXED WITH A PHOSPHORYLATED APC 20MER REPEAT.'''
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===THE CRYSTAL STRUCTURE OF BETA-CATENIN ARMADILLO REPEAT COMPLEXED WITH A PHOSPHORYLATED APC 20MER REPEAT.===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15327768}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15327768 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15327768}}
==About this Structure==
==About this Structure==
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[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Wnt signal]]
[[Category: Wnt signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:57:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:10:49 2008''

Revision as of 21:10, 27 July 2008

Image:1v18.png

Template:STRUCTURE 1v18

THE CRYSTAL STRUCTURE OF BETA-CATENIN ARMADILLO REPEAT COMPLEXED WITH A PHOSPHORYLATED APC 20MER REPEAT.

Template:ABSTRACT PUBMED 15327768

About this Structure

1V18 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. 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

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