Download MendeleyCrystal structure of the cell corpse engulfment protein CED-2 in Caenorhabditis elegans.
Kang, Y., Xu, J., Liu, Y., Sun, J., Sun, D., Hu, Y., Liu, Y.(2011) Biochem Biophys Res Commun 410: 189-194
- PubMed: 21616056
- DOI: https://doi.org/10.1016/j.bbrc.2011.05.051
- Primary Citation of Related Structures:
3QWX, 3QWY - PubMed Abstract:
In the nematode Caenorhabditis elegans, the cell corpse engulfment proteins CED-2, CED-5, and CED-12 act in the same pathway to regulate the activation of the Rac small GTPase, CED-10, leading to the rearrangement of the actin cytoskeleton for engulfing apoptotic cells. Nevertheless, it is not well understood how these proteins act together. Here we report the crystal structures of the CED-2 protein as determined by X-ray crystallography. The full-length CED-2 protein and its truncated form containing the N-terminal SH2 domain and the first SH3 domain show similar three-dimensional structures. A CED-2 point mutation (F125G) disrupting its interaction with the PXXP motif of CED-5 did not affect its rescuing activity. However, CED-2 was found to interact with the N-terminal region of CED-5. Our findings suggest that CED-2 may regulate cell corpse engulfment by interacting with CED-5 through the N-terminal region rather than the PXXP motif.
Organizational Affiliation:
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
