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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2001-12-13
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pubmed:databankReference |
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pubmed:abstractText |
Glycogen synthase kinase-3 (GSK-3) sequentially phosphorylates four serine residues on glycogen synthase (GS), in the sequence SxxxSxxxSxxx-SxxxS(p), by recognizing and phosphorylating the first serine in the sequence motif SxxxS(P) (where S(p) represents a phosphoserine). FRATtide (a peptide derived from a GSK-3 binding protein) binds to GSK-3 and blocks GSK-3 from interacting with Axin. This inhibits the Axin-dependent phosphorylation of beta-catenin by GSK-3.
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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/CDC2-CDC28 Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0969-2126
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pubmed:author |
pubmed-author:BanTT,
pubmed-author:BridgesAA,
pubmed-author:BrownM JMJ,
pubmed-author:CarterP SPS,
pubmed-author:CulbertA AAA,
pubmed-author:GuoA XAX,
pubmed-author:LewisCC,
pubmed-author:MannixCC,
pubmed-author:PettmanGG,
pubmed-author:ReithA DAD,
pubmed-author:SmithD GDG,
pubmed-author:TannerRR
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1143-52
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11738041-Amino Acid Motifs,
pubmed-meshheading:11738041-Amino Acid Sequence,
pubmed-meshheading:11738041-Animals,
pubmed-meshheading:11738041-Axin Protein,
pubmed-meshheading:11738041-Binding, Competitive,
pubmed-meshheading:11738041-Binding Sites,
pubmed-meshheading:11738041-CDC2-CDC28 Kinases,
pubmed-meshheading:11738041-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:11738041-Cell Line,
pubmed-meshheading:11738041-Crystallography, X-Ray,
pubmed-meshheading:11738041-Cyclin-Dependent Kinase 2,
pubmed-meshheading:11738041-Cyclin-Dependent Kinases,
pubmed-meshheading:11738041-Cytoskeletal Proteins,
pubmed-meshheading:11738041-Enzyme Activation,
pubmed-meshheading:11738041-Glycogen Synthase Kinase 3,
pubmed-meshheading:11738041-Glycogen Synthase Kinases,
pubmed-meshheading:11738041-Insects,
pubmed-meshheading:11738041-Kinetics,
pubmed-meshheading:11738041-Ligands,
pubmed-meshheading:11738041-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:11738041-Models, Molecular,
pubmed-meshheading:11738041-Molecular Sequence Data,
pubmed-meshheading:11738041-Peptides,
pubmed-meshheading:11738041-Phosphorylation,
pubmed-meshheading:11738041-Protein Binding,
pubmed-meshheading:11738041-Protein Structure, Secondary,
pubmed-meshheading:11738041-Protein Structure, Tertiary,
pubmed-meshheading:11738041-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11738041-Proteins,
pubmed-meshheading:11738041-Proto-Oncogene Proteins,
pubmed-meshheading:11738041-Repressor Proteins,
pubmed-meshheading:11738041-Sequence Homology, Amino Acid,
pubmed-meshheading:11738041-Serine,
pubmed-meshheading:11738041-Substrate Specificity,
pubmed-meshheading:11738041-Trans-Activators,
pubmed-meshheading:11738041-beta Catenin
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pubmed:year |
2001
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pubmed:articleTitle |
The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation.
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pubmed:affiliation |
Department of Structural Biology, GlaxoSmithKline Pharmaceuticals, Harlow, Essex CM19 5AD, United Kingdom. benjamin_d_bax@gsk.com
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pubmed:publicationType |
Journal Article
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