biostudies-literatureVallejo-Schmidt TNIGMS NIH HHS563-576https://www.ebi.ac.uk/biostudies/studies/S-EPMC11374754biostudies-literatureUnknown8(8)TLRs initiate innate immune signaling pathways via Toll/IL-1R (TIR) domains on their cytoplasmic tails. Various bacterial species also express TIR domain-containing proteins that contribute to bacterial evasion of the innate immune system. Bacterial TIR domains, along with the mammalian sterile α and TIR motif-containing protein 1 and TIRs from plants, also have been found to exhibit NADase activity. Initial X-ray crystallographic studies of the bacterial TIR from Acinetobacter baumannii provided insight into bacterial TIR structure but were unsuccessful in cocrystallization with the NAD+ ligand, leading to further questions about the TIR NAD binding site. In this study, we designed a Course-Based Undergraduate Research Experience (CURE) involving 16-20 students per year to identify amino ImmunoHorizonsCharacterization of the Structural Requirements for the NADase Activity of Bacterial Toll/IL-1R domains in a Course-based Undergraduate Research Experience.PMC11374754T32 GM146694R25 GM119970R25 GM058264Riedlbauer DWilliams ANVallejo-Schmidt TEromosele IRStefano AObiorah THamilton SDuff RJones JKSultana SSchmidt KSnyder GAChaudhry SSScudder AHPoteat AMShoemaker PRolle LTAWeldon JEGuzman-Cruz EPrice SEMercanti MASnyder MLDRiddick TFallah DKeshmiri NDavid JSterling MKRiaz TBader CDada TAConteh MToneygay LPascoe ERIngram LPAkingbehin VNallar SKoudjra ARErickson BCDe Leon RCalkins PHOjo MAPalm CAnderson JTCollins HAlexander ZOnwezi-Nwugwo JfalseCharacterization of the Structural Requirements for the NADase Activity of Bacterial Toll/IL-1R domains in a Course-based Undergraduate Research Experience.TLRs initiate innate immune signaling pathways via Toll/IL-1R (TIR) domains on their cytoplasmic tails. Various bacterial species also express TIR domain-containing proteins that contribute to bacterial evasion of the innate immune system. Bacterial TIR domains, along with the mammalian sterile α and TIR motif-containing protein 1 and TIRs from plants, also have been found to exhibit NADase activity. Initial X-ray crystallographic studies of the bacterial TIR from Acinetobacter baumannii provided insight into bacterial TIR structure but were unsuccessful in cocrystallization with the NAD+ ligand, leading to further questions about the TIR NAD binding site. In this study, we designed a Course-Based Undergraduate Research Experience (CURE) involving 16-20 students per year to identify amino 2024-01-01T00:00:00Z2024 Aug2026-06-01T12:13:24.828Z2024-11-15T21:29:20.616ZS-EPMC113747543917202610.4049/immunohorizons.2300062