ArticleProtein science : a publication of the Protein Society2003
Homology modeling provides insights into the binding mode of the PAAD/DAPIN/pyrin domain, a fourth member of the CARD/DD/DED domain family.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Pyrin- and CARD-only Proteins as Regulators of NLR Functions.Frontiers in immunology · 2013Review
- Structural and functional analysis of the NLRP4 pyrin domain.Biochemistry · 2012Article
- Uncoupling of Pyrin-only protein 2 (POP2)-mediated dual regulation of NF-κB and the inflammasome.The Journal of biological chemistry · 2011Article
- Systematic assessment of accuracy of comparative model of proteins belonging to different structural fold classes.Journal of molecular modeling · 2011Article
- IFI16 is an innate immune sensor for intracellular DNA.Nature immunology · 2010Article
- Three-dimensional structure of the NLRP7 pyrin domain: insight into pyrin-pyrin-mediated effector domain signaling in innate immunity.The Journal of biological chemistry · 2010Article
- Article
- Systematic analysis of the effect of multiple templates on the accuracy of comparative models of protein structure.BMC structural biology · 2008Article
- The PYRIN domain in signal transduction.Current protein & peptide science · 2007Review
- Accuracy of structure-derived properties in simple comparative models of protein structures.Nucleic acids research · 2005Article
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4 authors.
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Abstract
The PAAD/DAPIN/pyrin domain is the fourth member of the death domain superfamily, but unlike other members of this family, it is involved not only in apoptosis but also in innate immunity and several other processes. We have identified 40 PAAD domain-containing proteins by extensively searching the genomes of higher eukaryotes and viruses. Phylogenetic analyses suggest that there are five categories of PAAD domains that correlate with the domain architecture of the entire proteins. Homology models built on CARD and DD structures identified functionally important residues by studying conservation patterns on the surface of the models. Surface maps of each subfamily show different distributions of these residues, suggesting that domains from different subfamilies do not interact with each other, forming independent regulatory networks. Helix3 of PAAD is predicted to be critical for dimerization. Multiple alignment analysis and modeling suggest that it may be partly disordered, following a new paradigm for interaction proteins that are stabilized by protein-protein interactions.
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