Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain

By Zhihong Liu, Chaohong Sun, E. Olejniczak, R. Meadows, S. Betz, T. Oost, J. Herrmann, Joe C. Wu, Stephen W. Fesik. Nature, 2000

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Toxic proteins released from mitochondria in cell death (2004, background): “Structural analysis has revealed that the four N-terminal amino acids of Smac tether to a hydrophobic surface groove on the BIR3 domain of XIAP (Liu et al., 2000; Wu et al., 2000).”
Promoting apoptosis as a strategy for cancer drug discovery (2005, background): “SMAC, once released from the mitochondria, binds to the XIAP-BIR3 domai”
Mechanisms of caspase activation and inhibition during apoptosis. (2002, background): “In protein (Wu et al., 2000) or a nine residue Smac peptide (Liu et al., 2000).”
Intrinsically disordered proteins in human diseases: introducing the D2 concept. (2008, methodology): “(e) A ribbon diagram of the XIAP and Smac fragment complex was regenerated from PDB 1G3F (87).”
IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer (2010, background): “Type I BIR domains lack a peptide-binding groove, or possess a shallow pocket only, whereas type II BIRs carry a distinctive hydrophobic cleft through which they bind to N-terminal tetrapeptides called IAP-binding motifs (IBMs”
Viruses and apoptosis (2001, background): “This protein is normally resident in the mitochondria and is released into the cytosol following MPP, where it binds to IAP proteins in a structure that has already been defined by crystallography (Wu et al. 2000; Liu et al. 2000).”