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1q4q
From Proteopedia
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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 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
Page seeded by OCA on Thu Feb 21 14:35:49 2008
Categories: Drosophila melanogaster | Protein complex | Chai, J. | Shi, Y. | Yan, N. | ZN | Apoptosis | Caspase | Iap | Mechanism | Ubiquitination
