1D2Z

Three-dimensional structure of a complex between the death domains of Pelle and Tube.

(1999) Cell 99: 545-555

• PubMed: 10589682 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1016/s0092-8674(00)81542-1
• Primary Citation of Related Structures:  
  1D2Z


• PubMed Abstract: 
  

  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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Organizational Affiliation: 

The Howard Hughes Medical Institute and Department of Biochemistry, The University of Texas Southwestern Medical Center, Dallas 75235-9050, USA.