1jd4 | pdb_00001jd4

Crystal Structure of DIAP1-BIR2

spinqualitylabelsall models 1jd4, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1jd4 is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 1jd5, 1jd6 Gene: DIAP1 (DROME) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [IAP1_DROME] Anti-apoptotic protein which functions as a caspase regulator, using its E3 ubiquitin-protein ligase activity to smother caspase activity. Binds, ubiquitinates and inactivates initiator caspase Nc, and effector caspases ICE and DCP-1. Acts as a NEDD8-E3 ubiquitin-protein ligase for ICE. Suppresses apoptosis by targeting the apoptosome for ubiquitination and inactivation. Plays an important role in cell motility. Overexpression suppresses rpr and W-dependent cell death in the eye. Interaction of th with Nc is required to suppress Nc-mediated cell death; th-mediated ubiquitination of Nc. Acts as a positive regulator of Wnt signaling. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The inhibitor of apoptosis protein DIAP1 suppresses apoptosis in Drosophila, with the second BIR domain (BIR2) playing an important role. Three proteins, Hid, Grim, and Reaper, promote apoptosis, in part by binding to DIAP1 through their conserved N-terminal sequences. The crystal structures of DIAP1-BIR2 by itself and in complex with the N-terminal peptides from Hid and Grim reveal that these peptides bind a surface groove on DIAP1, with the first four amino acids mimicking the binding of the Smac tetrapeptide to XIAP. The next 3 residues also contribute to binding through hydrophobic interactions. Interestingly, peptide binding induces the formation of an additional alpha helix in DIAP1. Our study reveals the structural conservation and diversity necessary for the binding of IAPs by the Drosophila Hid/Grim/Reaper and the mammalian Smac proteins. Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides.,Wu JW, Cocina AE, Chai J, Hay BA, Shi Y Mol Cell. 2001 Jul;8(1):95-104. PMID:11511363 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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