1q4q

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Revision as of 22:15, 20 November 2007

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spinqualitylabelsall models 1q4q, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of a DIAP1-Dronc complex

Overview

The inhibitor of apoptosis protein DIAP1 inhibits Dronc-dependent cell, death by ubiquitinating Dronc. The pro-death proteins Reaper, Hid and Grim, (RHG) promote apoptosis by antagonizing DIAP1 function. Here we report the, structural basis of Dronc recognition by DIAP1 as well as a novel, mechanism by which the RHG proteins remove DIAP1-mediated downregulation, of Dronc. Biochemical and structural analyses revealed that the second BIR, (BIR2) domain of DIAP1 recognizes a 12-residue sequence in Dronc. This, recognition is essential for DIAP1 binding to Dronc, and for targeting, Dronc for ubiquitination. Notably, the Dronc-binding surface on BIR2, coincides with that required for binding to the N termini of the RHG, proteins, which competitively eliminate DIAP1-mediated ubiquitination of, Dronc. These observations reveal the molecular mechanisms of how DIAP1, recognizes Dronc, and more importantly, how the RHG proteins remove, DIAP1-mediated ubiquitination of Dronc.

About this Structure

1Q4Q is a Protein complex structure of sequences from Drosophila melanogaster with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination., Chai J, Yan N, Huh JR, Wu JW, Li W, Hay BA, Shi Y, Nat Struct Biol. 2003 Nov;10(11):892-8. Epub 2003 Sep 28. PMID:14517550

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