1v18: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1v18.gif|left|200px]]
{{Seed}}
[[Image:1v18.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1v18|  PDB=1v18  |  SCENE=  }}  
{{STRUCTURE_1v18|  PDB=1v18  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_15327768}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15327768 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15327768}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Wnt signal]]
[[Category: Wnt signal]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:57:42 2008''
 
''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

File: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

Page seeded by OCA on Mon Jul 28 00:10:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1v18&oldid=672836"