rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2001-1-10
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pubmed:databankReference |
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pubmed:abstractText |
The Wnt signaling pathway plays critical roles in embryonic development and tumorigenesis. Stimulation of the Wnt pathway results in the accumulation of a nuclear beta-catenin/Tcf complex, activating Wnt target genes. A crystal structure of beta-catenin bound to the beta-catenin binding domain of Tcf3 (Tcf3-CBD) has been determined. The Tcf3-CBD forms an elongated structure with three binding modules that runs antiparallel to beta-catenin along the positively charged groove formed by the armadillo repeats. Structure-based mutagenesis defines three sites in beta-catenin that are critical for binding the Tcf3-CBD and are differentially involved in binding APC, cadherin, and Axin. The structural and mutagenesis data reveal a potential target for molecular drug design studies.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Axin Protein,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HMGB Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TCF Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/TCF7L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor 7-Like 1...,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/axin1 protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/beta-catenin protein, Xenopus
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0092-8674
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
885-96
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11136974-Amino Acid Motifs,
pubmed-meshheading:11136974-Amino Acid Sequence,
pubmed-meshheading:11136974-Animals,
pubmed-meshheading:11136974-Axin Protein,
pubmed-meshheading:11136974-Cadherins,
pubmed-meshheading:11136974-Crystallography, X-Ray,
pubmed-meshheading:11136974-Cytoskeletal Proteins,
pubmed-meshheading:11136974-HMGB Proteins,
pubmed-meshheading:11136974-Humans,
pubmed-meshheading:11136974-Models, Molecular,
pubmed-meshheading:11136974-Molecular Sequence Data,
pubmed-meshheading:11136974-Mutagenesis, Site-Directed,
pubmed-meshheading:11136974-Precipitin Tests,
pubmed-meshheading:11136974-Protein Binding,
pubmed-meshheading:11136974-Protein Conformation,
pubmed-meshheading:11136974-Proteins,
pubmed-meshheading:11136974-Repressor Proteins,
pubmed-meshheading:11136974-Sequence Alignment,
pubmed-meshheading:11136974-Signal Transduction,
pubmed-meshheading:11136974-TCF Transcription Factors,
pubmed-meshheading:11136974-Trans-Activators,
pubmed-meshheading:11136974-Transcription Factor 7-Like 1 Protein,
pubmed-meshheading:11136974-Transcription Factors,
pubmed-meshheading:11136974-Xenopus,
pubmed-meshheading:11136974-Xenopus Proteins,
pubmed-meshheading:11136974-beta Catenin
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pubmed:year |
2000
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pubmed:articleTitle |
Crystal structure of a beta-catenin/Tcf complex.
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pubmed:affiliation |
Department of Biological Structure University of Washington 98195, Seattle, WA, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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