CADDomains present in proteins implicated in post-mortem DNA fragmentation
|SMART accession number:||SM00266|
|Interpro abstract (IPR003508):|
The CIDE-N or CAD domain is a ~78 amino acid protein-protein interaction domain in the N-terminal part of Cell death-Inducing DFF45-like Effector (CIDE) proteins, involved in apoptosis. At the final stage of programmed cell death, chromosomal DNA is degraded into fragments by Caspase-activated DNase (CAD), also named DNA fragmentation factor 40 kDa (DFF40). In normal cells CAD/DFF40 is completely inhibited by its binding to DFF45 or Inhibitor of CAD (ICAD). Apoptotic stimuli provoke cleavage of ICAD/DFF45 by caspases, resulting in self-assembly of CAD/DFF40 into the active dimer [(PUBMED:15149602)].
Both CAD/DFF40 and ICAD/DFF45 possess an N-terminal CIDE-N domain that is involved in their interaction. The name of the CIDE-N domain refers to the CIDE proteins and CAD, where the domain forms the N-terminal part [(PUBMED:9564035), (PUBMED:10619428)]. The CIDE-N domains from different proteins can interact, e.g. CIDE-N of CIDE-B and ICAD/DFF45 with CIDE-N of CAD/DFF40, and such interactions can also be needed for proper folding [(PUBMED:10764577), (PUBMED:11371636)].
Tertiary structures show that the CIDE-N domain forms an alpha/beta roll fold of five beta-strands forming a single, mixed parallel/anti-parallel beta-sheet with one [(PUBMED:10764577)] or two [(PUBMED:10619428), (PUBMED:11371636)] alpha-helices packed against the sheet. Binding surfaces of the CIDE-N domain form a central hydrophobic cluster, while specific binding interfaces can be formed by charged patches.
Some proteins known to contain a CIDE-N domain include:
|GO process:||apoptotic process (GO:0006915)|
|GO component:||intracellular (GO:0005622)|
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- Evolution (species in which this domain is found)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)