1Q4Q

Crystal structure of a DIAP1-Dronc complex

Summary for 1Q4Q

• Entry DOI: 10.2210/pdb1q4q/pdb
• Related: 1JD4 1JD5 1JD6
• Descriptor: Apoptosis 1 inhibitor, Nedd2-like caspase CG8091-PA, ZINC ION, ... (4 entities in total)
• Functional Keywords: caspase, iap, ubiquitination, apoptosis, apoptosis inhibitor
• Biological source: Drosophila melanogaster (fruit fly); More
• Total number of polymer chains: 20
• Total formula weight: 156187.92

Authors

Chai, J.,Yan, N.,Shi, Y. (deposition date: 2003-08-04, release date: 2003-11-04, Last modification date: 2024-02-14)

Primary citation

Chai, J.,Yan, N.,Huh, J.R.,Wu, J.-W.,Li, W.,Hay, B.A.,Shi, Y.
Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination
Nat.Struct.Biol., 10:892-898, 2003

PubMed Abstract: 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.

PubMed: 14517550
DOI: 10.1038/nsb989

Experimental method

X-RAY DIFFRACTION (2.1 Å)