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- W2044796693 abstract "Apoptosis and inflammation are important cellular processes that are highly regulated through specific protein-protein interactions (PPI). Proteins involved in these signaling cascades often carry PPI domains that belong to the death-domain superfamily. This includes the structurally well-characterized Death Domain (DD), the Death Effector Domain (DED) and the Caspase Recruitment Domain (CARD) subfamilies. Recently, a fourth member of the DD superfamily was identified, the Pyrin Domain (PYD). Based on sequence alignments, homology to other domains occurring in death-signalling pathways, and secondary-structure prediction, the PYD was predicted to have an overall fold similar to other DD superfamily members. Just recently, NMR structures of two PYDs have been determined. The PYD structures not only revealed the DD superfamily fold as previously predicted, but also distinct features that are characteristic exclusively for this subfamily. This review summarizes recent findings and developments regarding structural aspects of the DD superfamily, with a special emphasis on the PPIs of the DD superfamily." @default.
- W2044796693 created "2016-06-24" @default.
- W2044796693 creator A5045211499 @default.
- W2044796693 creator A5050745914 @default.
- W2044796693 date "2004-12-01" @default.
- W2044796693 modified "2023-09-30" @default.
- W2044796693 title "Fire and death: the pyrin domain joins the death-domain superfamily" @default.
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- W2044796693 doi "https://doi.org/10.1016/j.crvi.2004.08.006" @default.
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