@article{168461,
  keywords = {Animals, Models, Molecular, Protein Conformation, Crystallography, X-Ray, Mutation, Molecular Sequence Data, Repressor Proteins, Protein Binding, Recombinant Fusion Proteins, Amino Acid Sequence, Sequence Homology, Amino Acid, Conserved Sequence, Protein Structure, Secondary, Caenorhabditis elegans Proteins, Calcium-Binding Proteins, Transgenes, Electrophoresis, Polyacrylamide Gel, Apoptosis, Proto-Oncogene Proteins, Apoptosis Regulatory Proteins, Hydrogen Bonding, Proto-Oncogene Proteins c-bcl-2},
  author = {Nieng Yan and Lichuan Gu and David Kokel and Jijie Chai and Wenyu Li and Aidong Han and Lin Chen and Ding Xue and Yigong Shi},
  title = {Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4},
  abstract = {<p>Programmed cell death in Caenorhabditis elegans is initiated by the binding of EGL-1 to CED-9, which disrupts the CED-4/CED-9 complex and allows CED-4 to activate the cell-killing caspase CED-3. Here we demonstrate that the C-terminal half of EGL-1 is necessary and sufficient for binding to CED-9 and for killing cells. Structure of the EGL-1/CED-9 complex revealed that EGL-1 adopts an extended alpha-helical conformation and induces substantial structural rearrangements in CED-9 upon binding. EGL-1 interface mutants failed to bind to CED-9 or to release CED-4 from the CED-4/CED-9 complex, and were unable to induce cell death in vivo. A surface patch on CED-9, different from that required for binding to EGL-1, was identified to be responsible for binding to CED-4. These data suggest a working mechanism for the release of CED-4 from the CED-4/CED-9 complex upon EGL-1 binding and provide a mechanistic framework for understanding apoptosis activation in C. elegans.</p>
},
  year = {2004},
  journal = {Mol Cell},
  volume = {15},
  pages = {999-1006},
  month = {09/2004},
  issn = {1097-2765},
  doi = {10.1016/j.molcel.2004.08.022},
  language = {eng},
}