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. 2021 Apr 9;12(9):680–694. doi: 10.1007/s13238-021-00839-6

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© The Author(s) 2021

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Death domain structures and their interactions. (A) Structures of Fas DD (PDB ID: 1DDF), FADD DED (PDB ID: 2GF5), caspase-9 CARD (PDB ID: 3YGS), and ASC PYD (PDB ID: 3J63) show a characteristic six-helix bundle organization conserved in the DD superfamily. (B) Type I interaction revealed by the crystal structure of the Apaf-1 CARD-caspase-9 CARD complex (PDB ID: 3YGS). (C) Type II interaction uncovered by the crystal structure of the Pelle DD-Tube DD complex (PDB ID: 1D2Z). (D) Type III interaction defined by the crystal structure of the RAID DD-PIDD DD complex (PDB ID: 2OF5)