ArticleThe Journal of biological chemistry2010
Three-dimensional structure of the NLRP7 pyrin domain: insight into pyrin-pyrin-mediated effector domain signaling in innate immunity.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Article
- Pattern Recognition by NOD-Like Receptors.Advances in experimental medicine and biology · 2025Review
- The role of inflammasomes in human diseases and their potential as therapeutic targets.Signal transduction and targeted therapy · 2024Review
- Directionality of PYD filament growth determined by the transition of NLRP3 nucleation seeds to ASC elongation.Science advances · 2022Article
- Reproductive Outcomes from Maternal Loss of Nlrp2 Are Not Improved by IVF or Embryo Transfer Consistent with Oocyte-Specific Defect.Reproductive sciences (Thousand Oaks, Calif.) · 2021Article
- Structure, Activation and Regulation of NLRP3 and AIM2 Inflammasomes.International journal of molecular sciences · 2021Review
- ATP-Binding and Hydrolysis in Inflammasome Activation.Molecules (Basel, Switzerland) · 2020Review
- Genetic Aberrations Associated with Photodynamic Therapy in Colorectal Cancer Cells.International journal of molecular sciences · 2019Article
- Molecular mechanism for NLRP6 inflammasome assembly and activation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Hepatic toxicity following actinomycin D chemotherapy in treatment of familial gestational trophoblastic neoplasia: A case report.Medicine · 2018Article
- Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction.PloS one · 2018Article
- NLRP7 contributes to in vitro decidualization of endometrial stromal cells.Reproductive biology and endocrinology : RB&E · 2017Article
- Assembly and regulation of ASC specks.Cellular and molecular life sciences : CMLS · 2017Review
- Inflammasomes in Myeloid Cells: Warriors Within.Microbiology spectrum · 2017Review
- ASC Pyrin Domain Self-associates and Binds NLRP3 Protein Using Equivalent Binding Interfaces.The Journal of biological chemistry · 2016Article
- Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF).BMB reports · 2016Review
- Inhibiting the inflammasome: one domain at a time.Immunological reviews · 2015Review
- The hierarchical structural architecture of inflammasomes, supramolecular inflammatory machines.Current opinion in structural biology · 2015Review
- An updated view on the structure and function of PYRIN domains.Apoptosis : an international journal on programmed cell death · 2015Article
- Intrinsic flexibility of NLRP pyrin domains is a key factor in their conformational dynamics, fold stability, and dimerization.Protein science : a publication of the Protein Society · 2015Article
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6 authors.
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Abstract
The innate immune system provides an initial line of defense against infection. Nucleotide-binding domain- and leucine-rich repeat-containing protein (NLR or (NOD-like)) receptors play a critical role in the innate immune response by surveying the cytoplasm for traces of intracellular invaders and endogenous stress signals. NLRs themselves are multi-domain proteins. Their N-terminal effector domains (typically a pyrin or caspase activation and recruitment domain) are responsible for driving downstream signaling and initiating the formation of inflammasomes, multi-component complexes necessary for cytokine activation. However, the currently available structures of NLR effector domains have not yet revealed the mechanism of their differential modes of interaction. Here, we report the structure and dynamics of the N-terminal pyrin domain of NLRP7 (NLRP7 PYD) obtained by NMR spectroscopy. The NLRP7 PYD adopts a six-alpha-helix bundle death domain fold. A comparison of conformational and dynamics features of the NLRP7 PYD with other PYDs showed distinct differences for helix alpha3 and loop alpha2-alpha3, which, in NLRP7, is stabilized by a strong hydrophobic cluster. Moreover, the NLRP7 and NLRP1 PYDs have different electrostatic surfaces. This is significant, because death domain signaling is driven by electrostatic contacts and stabilized by hydrophobic interactions. Thus, these results provide new insights into NLRP signaling and provide a first molecular understanding of inflammasome formation.
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