1m1e: Difference between revisions

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1e OCA], [http://www.ebi.ac.uk/pdbsum/1m1e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m1e RCSB]</span>
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[[Category: transciption factor]]
[[Category: transciption factor]]


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Revision as of 22:10, 30 March 2008

File:1m1e.gif


PDB ID 1m1e

Drag the structure with the mouse to rotate
, resolution 2.10Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Beta-catenin armadillo repeat domain bound to ICAT


OverviewOverview

In the canonical Wnt signaling pathway, beta-catenin activates target genes through its interactions with Tcf/Lef-family transcription factors and additional transcriptional coactivators. The crystal structure of ICAT, an inhibitor of beta-catenin-mediated transcription, bound to the armadillo repeat domain of beta-catenin, has been determined. ICAT contains an N-terminal helilical domain that binds to repeats 11 and 12 of beta-catenin, and an extended C-terminal region that binds to repeats 5-10 in a manner similar to that of Tcfs and other beta-catenin ligands. Full-length ICAT dissociates complexes of beta-catenin, Lef-1, and the transcriptional coactivator p300, whereas the helical domain alone selectively blocks binding to p300. The C-terminal armadillo repeats of beta-catenin may be an attractive target for compounds designed to disrupt aberrant beta-catenin-mediated transcription associated with various cancers.

About this StructureAbout this Structure

1M1E is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules., Daniels DL, Weis WI, Mol Cell. 2002 Sep;10(3):573-84. PMID:12408825

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