1ty4
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Crystal structure of a CED-9/EGL-1 complex
OverviewOverview
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.
About this StructureAbout this Structure
1TY4 is a Protein complex structure of sequences from Caenorhabditis elegans. Full crystallographic information is available from OCA.
ReferenceReference
Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4., Yan N, Gu L, Kokel D, Chai J, Li W, Han A, Chen L, Xue D, Shi Y, Mol Cell. 2004 Sep 24;15(6):999-1006. PMID:15383288
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