CRYSTAL STRUCTURE OF THE CED-9/CED-4/CED-3 TERNARY COMPLEX

$17,043P41FY2009RRNIH

Brookhaven Science Assoc-Brookhaven Lab, Upton NY

Investigators

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Abstract

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Apoptosis plays an essential role in the development and homeostasis of metazoans. The genetic characterization of programmed cell death (apoptosis) in C. elegans identified four proteins, CED-3, CED-4, CED-9, and EGL-1, that collectively control the onset of apoptosis. CED-3 is a caspase and its activation depends on CED-4. CED-9 antagonize the function of CED-4 through an unknown mechanism. CED-3, CED-4, and CED-9 form a hetero-oligomer. To elucidate the mechanisms of cell death control in C. elegans, we crystallized the ternary complex of CED-3/CED-4/CED-9. We plan to determine the structure by molecular replacement or by MAD.

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