|PROSITE documentation PDOC51135 [for PROSITE entry PS51135]|
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 .
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 [2,3]. 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 [4,5].
Tertiary structures show that the CIDE-N domain forms an α/β roll fold of five β-strands forming a single, mixed parallel/anti-parallel β-sheet with one  or two [3,5] α-helices packed against the sheet (see <PDB:1IBX>). 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:
The profile we developed covers the entire CIDE-N domain.Last update:
June 2005 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Woo E.J. Kim Y.G. Kim M.S. Han W.D. Shin S. Robinson H. Park S.Y. Oh B.H.|
|Title||Structural mechanism for inactivation and activation of CAD/DFF40 in the apoptotic pathway.|
|Source||Mol. Cell 14:531-539(2004).|
|2||Authors||Inohara N. Koseki T. Chen S. Wu X. Nunez G.|
|Title||CIDE, a novel family of cell death activators with homology to the 45 kDa subunit of the DNA fragmentation factor.|
|Source||EMBO J. 17:2526-2533(1998).|
|3||Authors||Lugovskoy A.A. Zhou P. Chou J.J. McCarty J.S. Li P. Wagner G.|
|Title||Solution structure of the CIDE-N domain of CIDE-B and a model for CIDE-N/CIDE-N interactions in the DNA fragmentation pathway of apoptosis.|
|4||Authors||Uegaki K. Otomo T. Sakahira H. Shimizu M. Yumoto N. Kyogoku Y. Nagata S. Yamazaki T.|
|Title||Structure of the CAD domain of caspase-activated DNase and interaction with the CAD domain of its inhibitor.|
|Source||J. Mol. Biol. 297:1121-1128(2000).|
|5||Authors||Zhou P. Lugovskoy A.A. McCarty J.S. Li P. Wagner G.|
|Title||Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 98:6051-6055(2001).|