1m1e: Difference between revisions
New page: left|200px<br /> <applet load="1m1e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m1e, resolution 2.10Å" /> '''Beta-catenin armadi... |
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[[Image:1m1e.gif|left|200px]]<br /> | [[Image:1m1e.gif|left|200px]]<br /><applet load="1m1e" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1m1e, resolution 2.10Å" /> | caption="1m1e, resolution 2.10Å" /> | ||
'''Beta-catenin armadillo repeat domain bound to ICAT'''<br /> | '''Beta-catenin armadillo repeat domain bound to ICAT'''<br /> | ||
==Overview== | ==Overview== | ||
In the canonical Wnt signaling pathway, beta-catenin activates target | 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 Structure== | ==About this Structure== | ||
1M1E is a [http://en.wikipedia.org/wiki/Protein_complex 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:// | 1M1E is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Daniels, D | [[Category: Daniels, D L.]] | ||
[[Category: Weis, W | [[Category: Weis, W I.]] | ||
[[Category: armadillo repeats]] | [[Category: armadillo repeats]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
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[[Category: transciption factor]] | [[Category: transciption factor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:28 2008'' | ||
Revision as of 14:50, 21 February 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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