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
2012
Structural Insights into the Substrate Specificity of Human Granzyme H: The Functional Roles of a Novel RKR Motif
Wang L, Zhang K, Wu L, Liu S, Zhang H, Zhou Q, Tong L, Sun F, Fan Z. Structural Insights into the Substrate Specificity of Human Granzyme H: The Functional Roles of a Novel RKR Motif. The Journal Of Immunology 2012, 188: 765-773. PMID: 22156497, DOI: 10.4049/jimmunol.1101381.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsCatalytic DomainCatsCell LineCell Line, TransformedCrystallography, X-RayCytotoxicity, ImmunologicDogsGranzymesHumansHydrogen-Ion ConcentrationK562 CellsMolecular Sequence DataPan troglodytesProtein BindingSerine Proteinase InhibitorsSubstrate SpecificityConceptsRKR motifHuman granzyme HStructural insightsSubstrate recognition mechanismChymotrypsin-like serine proteaseGranzyme HSubstrate recognitionSubstrate specificitySubstrate preferenceChloromethylketone inhibitorAcidic residuesInnate immune responseAromatic residuesFunctional roleP1 positionSerine proteasesS1 pocketRecognition mechanismMotifGzmHResiduesProteolytic activityDecapeptide substrateImportant roleMutants