1d2z
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(New page: 200px<br /><applet load="1d2z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d2z, resolution 2.0Å" /> '''THREE-DIMENSIONAL STR...)
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Revision as of 10:51, 20 November 2007
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THREE-DIMENSIONAL STRUCTURE OF A COMPLEX BETWEEN THE DEATH DOMAINS OF PELLE AND TUBE
Overview
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.
About this Structure
1D2Z is a Protein complex structure of sequences from Drosophila melanogaster with EPE as ligand. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of a complex between the death domains of Pelle and Tube., Xiao T, Towb P, Wasserman SA, Sprang SR, Cell. 1999 Nov 24;99(5):545-55. PMID:10589682
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