Structural and Functional Analysis of the NLRP4 Pyrin Domain

@inproceedings{Eibl2012StructuralAF,
  title={Structural and Functional
Analysis of the NLRP4 Pyrin
Domain},
  author={Clarissa Eibl and Simina Grigoriu and Manuel Hessenberger and Julia Wenger and Sandra Puehringer and A. Pinheiro and Roland N. Wagner and Martina Proell and John C. Reed and Rebecca Page and Kay Diederichs and Wolfgang Peti},
  booktitle={Biochemistry},
  year={2012}
}
NLRP4 is a member of the nucleotide-binding and leucine-rich repeat receptor (NLR) family of cytosolic receptors and a member of an inflammation signaling cascade. Here, we present the crystal structure of the NLRP4 pyrin domain (PYD) at 2.3 Å resolution. The NLRP4 PYD is a member of the death domain (DD) superfamily and adopts a DD fold consisting of six α-helices tightly packed around a hydrophobic core, with a highly charged surface that is typical of PYDs. Importantly, however, we… CONTINUE READING