2020
NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation
Leng F, Yin H, Qin S, Zhang K, Guan Y, Fang R, Wang H, Li G, Jiang Z, Sun F, Wang DC, Xie C. NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation. Scientific Reports 2020, 10: 198. PMID: 31932628, PMCID: PMC6957519, DOI: 10.1038/s41598-019-57043-0.Peer-Reviewed Original ResearchConceptsNOD-like receptorsGlobal conformational changesStep-activation mechanismOuter membraneMolecular platformStructural basisAssembly patternsLigand specificityConformational changesInnate immune responseImmune receptorsActivation mechanismIntestinal homeostasisNegative bacteriaATP stimulationPathogen productsIntestinal tumorigenesisHigher molecular structuresMajor componentNLRP6Important roleHomodimerReceptorsCytosolImmune response
2013
Structure Reveals Regulatory Mechanisms of a MaoC-Like Hydratase from Phytophthora capsici Involved in Biosynthesis of Polyhydroxyalkanoates (PHAs)
Wang H, Zhang K, Zhu J, Song W, Zhao L, Zhang X. Structure Reveals Regulatory Mechanisms of a MaoC-Like Hydratase from Phytophthora capsici Involved in Biosynthesis of Polyhydroxyalkanoates (PHAs). PLOS ONE 2013, 8: e80024. PMID: 24244597, PMCID: PMC3823801, DOI: 10.1371/journal.pone.0080024.Peer-Reviewed Original ResearchAcyl Coenzyme AAmino Acid SequenceBinding SitesBiocatalysisCatalytic DomainCrystallography, X-RayEnoyl-CoA HydrataseEscherichia coliModels, MolecularMolecular Sequence DataMutationOxidation-ReductionPhytophthoraPolyhydroxyalkanoatesProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidSubstrate Specificity