Antagonists Induce a Conformational Change in cIAP1 That Promotes Autoubiquitination

• DOI: 10.1126/science.1207862
• Publication Date: 2011-10-20T18:47:20Z
• Authors: Erin C. Dueber; Allyn J. Schoeffler; Andreas Lingel; J. Michael Elliott; Anna V. Fedorova; Anthony M. Giannetti; Kerry Zobel; Brigitte Maurer; Eugene Varfolomeev; Ping Wu; Heidi J. A. Wallw...; Sarah G. Hymowitz; Kurt Deshayes; Domagoj Vucic; Wayne J. Fairbrother
• Keywords: Models, Molecular; Proteasome Endopeptidase Complex; 0303 health sciences; Protein Conformation; Ubiquitin-Protein Ligases; Molecular Sequence Data; Models, Biological; Protein Structure, Secondary; Cell Line; Inhibitor of Apoptosis Proteins; 3. Good health; Mice; 03 medical and health sciences; Cell Line, Tumor; Scattering, Small Angle; Mutagenesis, Site-Directed; Animals; Humans; Protein Interaction Domains and Motifs; Amino Acid Sequence; Cloning, Molecular; Protein Multimerization; Hydrophobic and Hydrophilic Interactions

Antagonist binding to an apoptosis inhibitor releases inhibition by promoting dimerization required for autoubiquitination.