1JD6

Crystal Structure of DIAP1-BIR2/Hid Complex

Summary for 1JD6

• Entry DOI: 10.2210/pdb1jd6/pdb
• Related: 1JD4 1JD5
• Descriptor: APOPTOSIS 1 INHIBITOR, head involution defective protein, ZINC ION (3 entities in total)
• Functional Keywords: apoptosis, iap, hid, caspase activation, drosophila, hydrolase-peptide complex, hydrolase/peptide
• Biological source: Drosophila melanogaster (fruit fly); More
• Total number of polymer chains: 2
• Total formula weight: 15193.28

Authors

Wu, J.W.,Cocina, A.E.,Chai, J.,Hay, B.A.,Shi, Y. (deposition date: 2001-06-12, release date: 2001-12-05, Last modification date: 2024-02-07)

Primary citation

Wu, J.W.,Cocina, A.E.,Chai, J.,Hay, B.A.,Shi, Y.
Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides.
Mol.Cell, 8:95-104, 2001

PubMed Abstract: 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.

PubMed: 11511363
DOI: 10.1016/S1097-2765(01)00282-9

Experimental method

X-RAY DIFFRACTION (2.7 Å)