2a90
From Proteopedia
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Crystal Structure of the tandem WWE domain of Drosophila Deltex
Overview
Deltex is a cytosolic effector of Notch signaling thought to bind through, its N-terminal domain to the Notch receptor. Here we report the structure, of the Drosophila Deltex N-terminal domain, which contains two tandem WWE, sequence repeats. The WWE repeats, which adopt a novel fold, are related, by an approximate two-fold axis of rotation. Although the WWE repeats are, structurally distinct, they interact extensively and form a deep cleft at, their junction that appears well suited for ligand binding. The two, repeats are thermodynamically coupled; this coupling is mediated in part, by a conserved segment that is immediately C-terminal to the second WWE, domain. We demonstrate that although the Deltex WWE tandem is monomeric in, solution, it forms a heterodimer with the ankyrin domain of the Notch, receptor. These results provide structural and functional insight into how, Deltex modulates Notch signaling, and how WWE modules recognize targets, for ubiquitination.
About this Structure
2A90 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Structure and Notch receptor binding of the tandem WWE domain of Deltex., Zweifel ME, Leahy DJ, Barrick D, Structure. 2005 Nov;13(11):1599-611. PMID:16271883
Page seeded by OCA on Wed Nov 21 07:59:31 2007
