PDBsum entry 3qwy

Signaling protein

PDB id: 3qwy

Contents

Protein chains

170 a.a.

Ligands

SO4

GOL

Waters ×128

PDB id:

3qwy

Name:

Signaling protein

Title:

Ced-2

Structure:

Cell death abnormality protein 2. Chain: a, b. Synonym: cell-corpse engulfment protein ced-2. Engineered: yes

Source:

Caenorhabditis elegans. Nematode. Organism_taxid: 6239. Gene: ced-2, y41d4b.13. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.52Å R-factor: 0.207 R-free: 0.268

Authors:

Y.Kang,J.Sun,Y.Liu,D.Sun,Y.Hu,Y.F.Liu

Key ref:

Y.Kang et al. (2011). Crystal structure of the cell corpse engulfment protein CED-2 in Caenorhabditis elegans. Biochem Biophys Res Commun, 410, 189-194. PubMed id: 21616056

Date:

28-Feb-11 Release date: 08-Jun-11

Protein chains

Q9NHC3  (CED2_CAEEL) -  Cell death abnormality protein 2 from Caenorhabditis elegans

Seq: 279 a.a.

Struc: 170 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Biochem Biophys Res Commun 410:189-194 (2011)

PubMed id: 21616056

Crystal structure of the cell corpse engulfment protein CED-2 in Caenorhabditis elegans.

Y.Kang, J.Xu, Y.Liu, J.Sun, D.Sun, Y.Hu, Y.Liu.

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.