2023
Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport
Ton W, Wang Y, Chai P, Beauchamp-Perez C, Flint N, Lammers L, Xiong H, Zhang K, Markus S. Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport. Nature Structural & Molecular Biology 2023, 30: 1365-1379. PMID: 37322240, PMCID: PMC10590275, DOI: 10.1038/s41594-023-01010-x.Peer-Reviewed Original ResearchMeSH KeywordsDyneinsHumansMicrotubule-Associated ProteinsMicrotubulesProtein BindingSaccharomyces cerevisiaeConceptsCryo-EM structureCargo transportProtein Lis1Human dyneinDynein mutantsCytoplasmic dyneinStructural insightsDynein activityIntracellular localizationCritical regulatorDynein activationLIS1Conformational changesDyneinMotor domainMutantsBindingHigh affinityAffinityYeastMicrotubulesRegulatorRegulationTransportActivation
2014
A PH Domain in ACAP1 Possesses Key Features of the BAR Domain in Promoting Membrane Curvature
Pang X, Fan J, Zhang Y, Zhang K, Gao B, Ma J, Li J, Deng Y, Zhou Q, Egelman EH, Hsu VW, Sun F. A PH Domain in ACAP1 Possesses Key Features of the BAR Domain in Promoting Membrane Curvature. Developmental Cell 2014, 31: 73-86. PMID: 25284369, PMCID: PMC4198613, DOI: 10.1016/j.devcel.2014.08.020.Peer-Reviewed Original Research
2013
Flexible interwoven termini determine the thermal stability of thermosomes
Zhang K, Wang L, Liu Y, Chan KY, Pang X, Schulten K, Dong Z, Sun F. Flexible interwoven termini determine the thermal stability of thermosomes. Protein & Cell 2013, 4: 432-444. PMID: 23709365, PMCID: PMC3740188, DOI: 10.1007/s13238-013-3026-9.Peer-Reviewed Original ResearchIdentification of SERPINB1 As a Physiological Inhibitor of Human Granzyme H
Wang L, Li Q, Wu L, Liu S, Zhang Y, Yang X, Zhu P, Zhang H, Zhang K, Lou J, Liu P, Tong L, Sun F, Fan Z. Identification of SERPINB1 As a Physiological Inhibitor of Human Granzyme H. The Journal Of Immunology 2013, 190: 1319-1330. PMID: 23269243, DOI: 10.4049/jimmunol.1202542.Peer-Reviewed Original ResearchCatalysisCell Line, TumorChromatography, GelCrystallography, X-RayCytoplasmic GranulesCytotoxicity, ImmunologicGenetic VectorsGranzymesHumansJurkat CellsKiller Cells, Lymphokine-ActivatedModels, MolecularNeoplasm ProteinsProtein BindingProtein ConformationProtein Interaction MappingRecombinant Fusion ProteinsSerpinsStructure-Activity RelationshipAtomic Model of Rabbit Hemorrhagic Disease Virus by Cryo-Electron Microscopy and Crystallography
Wang X, Xu F, Liu J, Gao B, Liu Y, Zhai Y, Ma J, Zhang K, Baker TS, Schulten K, Zheng D, Pang H, Sun F. Atomic Model of Rabbit Hemorrhagic Disease Virus by Cryo-Electron Microscopy and Crystallography. PLOS Pathogens 2013, 9: e1003132. PMID: 23341770, PMCID: PMC3547835, DOI: 10.1371/journal.ppat.1003132.Peer-Reviewed Original Research
2012
Mechanistic Insights into Regulated Cargo Binding by ACAP1 Protein*
Bai M, Pang X, Lou J, Zhou Q, Zhang K, Ma J, Li J, Sun F, Hsu VW. Mechanistic Insights into Regulated Cargo Binding by ACAP1 Protein*. Journal Of Biological Chemistry 2012, 287: 28675-28685. PMID: 22645133, PMCID: PMC3436524, DOI: 10.1074/jbc.m112.378810.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsCargo bindingIntegrin recyclingRegulated transportArf6 GTPase-activating ProteinsADP-ribosylation factor (ARF) familyVesicular transport pathwaysMechanistic insightsEndocytic recyclingCoat complexSmall GTPasesCytoplasmic domainCoat componentsFurther mechanistic insightsProtein cargoFactor familyACAP1Functional studiesIntegrin β1Critical sequencesPhosphorylationBindingTransport pathwaysProteinCargoStructural 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
2010
Crystal Structure of Group II Chaperonin in the Open State
Huo Y, Hu Z, Zhang K, Wang L, Zhai Y, Zhou Q, Lander G, Zhu J, He Y, Pang X, Xu W, Bartlam M, Dong Z, Sun F. Crystal Structure of Group II Chaperonin in the Open State. Structure 2010, 18: 1270-1279. PMID: 20947016, PMCID: PMC3048791, DOI: 10.1016/j.str.2010.07.009.Peer-Reviewed Original ResearchConceptsGroup II chaperoninLid domainConformational changesOpen stateATP-dependent mannerHigh-resolution structuresDetailed conformational changesFunctional cycleThermosomeHydrophobic patchStructural comparisonProtease K digestionChaperoninClosed stateK digestionCrystal structureStructural fittingOpen formComplete crystal structureClosed structureSpeciesDomainProteinATPElectron microscopy