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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1999-12-28
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pubmed:databankReference |
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pubmed:abstractText |
The interaction of the serine/threonine kinase Pelle and adaptor protein Tube through their N-terminal death domains leads to the nuclear translocation of the transcription factor Dorsal and activation of zygotic patterning genes during Drosophila embryogenesis. Crystal structure of the Pelle and Tube death domain heterodimer reveals that the two death domains adopt a six-helix bundle fold and are arranged in an open-ended linear array with plastic interfaces mediating their interactions. The Tube death domain has an insertion between helices 2 and 3, and a C-terminal tail making significant and indispensable contacts in the heterodimer. In vivo assays of Pelle and Tube mutants confirmed that the integrity of the major heterodimer interface is critical to the activity of these molecules.
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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/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/dl (dorsal) protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/pll protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/tube protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
545-55
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pubmed:dateRevised |
2008-10-15
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pubmed:meshHeading |
pubmed-meshheading:10589682-Amino Acid Sequence,
pubmed-meshheading:10589682-Binding Sites,
pubmed-meshheading:10589682-Cell Death,
pubmed-meshheading:10589682-Crystallization,
pubmed-meshheading:10589682-Crystallography,
pubmed-meshheading:10589682-Dimerization,
pubmed-meshheading:10589682-Drosophila Proteins,
pubmed-meshheading:10589682-Insect Proteins,
pubmed-meshheading:10589682-Models, Molecular,
pubmed-meshheading:10589682-Molecular Sequence Data,
pubmed-meshheading:10589682-Mutagenesis, Site-Directed,
pubmed-meshheading:10589682-NF-kappa B,
pubmed-meshheading:10589682-Nuclear Proteins,
pubmed-meshheading:10589682-Peptide Fragments,
pubmed-meshheading:10589682-Phosphoproteins,
pubmed-meshheading:10589682-Protein Binding,
pubmed-meshheading:10589682-Protein Structure, Tertiary,
pubmed-meshheading:10589682-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10589682-Sequence Homology, Amino Acid,
pubmed-meshheading:10589682-Transcription Factors
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pubmed:year |
1999
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pubmed:articleTitle |
Three-dimensional structure of a complex between the death domains of Pelle and Tube.
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pubmed:affiliation |
The Howard Hughes Medical Institute and Department of Biochemistry, The University of Texas Southwestern Medical Center, Dallas 75235-9050, 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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