Structural highlights
Function
[DFFB_MOUSE] Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology. [DFFA_MOUSE] Inhibitor of the caspase-activated DNase (DFF40).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We present here the structure of the complex between the CAD domain of caspase activated deoxyribonuclease (CAD) and the CAD domain of its inhibitor (ICAD), determined by nuclear magnetic resonance spectroscopy. The two domains adopt a very similar fold, which consists of an alpha-helix and a beta-sheet, and are aligned side by side in the complex. Notably, the positive charges on the strand beta2 at one end of the beta-sheet of CAD and negative charges around the opposite end of the beta-sheet of ICAD are paired in the complex. Point mutations of the charged amino acids at this interface, on either CAD or ICAD, prevented formation of the functional CAD-ICAD complex. This implies that the interaction between the CAD domains of CAD and ICAD is an essential step in the correct folding of CAD in the complex.
Structure of the heterodimeric complex between CAD domains of CAD and ICAD.,Otomo T, Sakahira H, Uegaki K, Nagata S, Yamazaki T Nat Struct Biol. 2000 Aug;7(8):658-62. PMID:10932250[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Otomo T, Sakahira H, Uegaki K, Nagata S, Yamazaki T. Structure of the heterodimeric complex between CAD domains of CAD and ICAD. Nat Struct Biol. 2000 Aug;7(8):658-62. PMID:10932250 doi:10.1038/77957
