Three-dimensional structure of a complex between the death domains of pelle and tube

Tsan Xiao, Par Towb, Steven A. Wasserman, Stephen R. Sprang

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)545-555
Number of pages11
JournalCell
Volume99
Issue number5
DOIs
StatePublished - Nov 24 1999

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