1m1e: Difference between revisions
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[[Image:1m1e.gif|left|200px]] | [[Image:1m1e.gif|left|200px]] | ||
'''Beta-catenin armadillo repeat domain bound to ICAT''' | {{Structure | ||
|PDB= 1m1e |SIZE=350|CAPTION= <scene name='initialview01'>1m1e</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Beta-catenin armadillo repeat domain bound to ICAT''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1M1E is a [ | 1M1E is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1E OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12408825 12408825] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: Daniels, D L.]] | [[Category: Daniels, D L.]] | ||
[[Category: Weis, W I.]] | [[Category: Weis, W I.]] | ||
[[Category: armadillo | [[Category: armadillo repeat]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
[[Category: cytoskeleton]] | [[Category: cytoskeleton]] | ||
[[Category: transciption factor]] | [[Category: transciption factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:37:42 2008'' | ||
Revision as of 13:37, 20 March 2008
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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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