Structures, Domains and Functions in Cell Death (DD, DED, CARD, PYD)
Published Online: 15 DEC 2009
Copyright © 2001 John Wiley & Sons, Ltd. All rights reserved.
How to Cite
Wu, H. and Lo, Y.-C. 2009. Structures, Domains and Functions in Cell Death (DD, DED, CARD, PYD). eLS.
- Published Online: 15 DEC 2009
The death domain (DD), death effector domain (DED), caspase-recruitment domain (CARD) and pyrin domain (PYD) are subfamilies of the DD superfamily. By mediating homotypic interactions, these proteins play important roles in the assembly and activation of apoptotic signalling complexes. They are responsible for caspase recruitment and for formation of oligomeric platforms for signalling. DD superfamily proteins have a common six-helical bundle fold and show different surface features for each of the subfamilies. Most interestingly, the homotypic interactions within each subfamily are mostly mediated by asymmetric contacts, in which different surfaces of the interaction partners are adjacent to each other. The DD superfamily proteins appear to use three common types of asymmetric interactions to assemble into large oligomeric complexes.
Death domains (DDs), death effector domains (DEDs), caspase-recruitment domains (CARDs) and pyrin domains (PYDs) are protein:protein interaction modules for formation of caspase-activating complexes.
DDs, DEDs, CARDs and PYDs share a common six-helical bundle fold.
Interactions within these domains are mostly asymmetric and conserved.
- death domain (DD);
- death effector domain (DED);
- tandem DED;
- caspase recruitment domain (CARD);
- pyrin domain (PYD);