2023
LRRC23 truncation impairs radial spoke 3 head assembly and sperm motility underlying male infertility
Hwang J, Chai P, Nawaz S, Choi J, Lopez-Giraldez F, Hussain S, Bilguvar K, Mane S, Lifton R, Ahmad W, Zhang K, Chung J. LRRC23 truncation impairs radial spoke 3 head assembly and sperm motility underlying male infertility. ELife 2023, 12: rp90095. PMID: 38091523, PMCID: PMC10721216, DOI: 10.7554/elife.90095.Peer-Reviewed Original ResearchMicrotubule-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 ResearchConceptsCryo-EM structureCargo transportProtein Lis1Human dyneinDynein mutantsCytoplasmic dyneinStructural insightsDynein activityIntracellular localizationCritical regulatorDynein activationLIS1Conformational changesDyneinMotor domainMutantsBindingHigh affinityAffinityYeastMicrotubulesRegulatorRegulationTransportActivation
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
2019
Structural basis of antagonism of human APOBEC3F by HIV-1 Vif
Hu Y, Desimmie BA, Nguyen HC, Ziegler SJ, Cheng TC, Chen J, Wang J, Wang H, Zhang K, Pathak VK, Xiong Y. Structural basis of antagonism of human APOBEC3F by HIV-1 Vif. Nature Structural & Molecular Biology 2019, 26: 1176-1183. PMID: 31792451, PMCID: PMC6899190, DOI: 10.1038/s41594-019-0343-6.Peer-Reviewed Original ResearchConceptsHIV-1 VifProtein degradation machineryCryo-EM structureHuman immunodeficiency virus type 1 (HIV-1) replicationCore-binding factor betaUbiquitin-proteasome pathwayRole of CbfβHIV-1 virion infectivity factorType 1 replicationVif-A3 interactionsViral immune evasionDegradation machineryAntiviral APOBEC3Terminal domainVirion infectivity factorStructural basisMolecular mechanismsViral restrictionA3 proteinsMolecular determinantsImmune evasionInfectivity factorFactor betaCellular studiesAntiviral therapeuticsNew interfaces on MiD51 for Drp1 recruitment and regulation
Ma J, Zhai Y, Chen M, Zhang K, Chen Q, Pang X, Sun F. New interfaces on MiD51 for Drp1 recruitment and regulation. PLOS ONE 2019, 14: e0211459. PMID: 30703167, PMCID: PMC6355003, DOI: 10.1371/journal.pone.0211459.Peer-Reviewed Original Research
2018
A brief introduction of cryo-EM revolution—the Nobel Prize in Chemistry 2017
Zhang K, Liu Z. A brief introduction of cryo-EM revolution—the Nobel Prize in Chemistry 2017. Science China Life Sciences 2018, 61: 368-370. PMID: 29318502, DOI: 10.1007/s11427-017-9215-3.Peer-Reviewed Original Research
2017
Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated
Zhang K, Foster HE, Rondelet A, Lacey SE, Bahi-Buisson N, Bird AW, Carter AP. Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated. Cell 2017, 169: 1303-1314.e18. PMID: 28602352, PMCID: PMC5473941, DOI: 10.1016/j.cell.2017.05.025.Peer-Reviewed Original ResearchConceptsStructure-based mutagenesisCryoelectron microscopy structureCargo adaptor proteinsMicroscopy structureAdaptor proteinCytoplasmic dyneinMicrotubule affinityCryo-EMDynein 1DynactinOpen formDynein tailInhibited stateProcessive movementMotor domainMicrotubulesMotor dimerizationTransport machinesHigh affinityMutagenesisDyneinTailAffinityProteinDimerization
2015
The structure of the dynactin complex and its interaction with dynein
Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP. The structure of the dynactin complex and its interaction with dynein. Science 2015, 347: 1441-1446. PMID: 25814576, PMCID: PMC4413427, DOI: 10.1126/science.aaa4080.Peer-Reviewed Original ResearchConceptsDynactin complexBicaudal D2Microtubule motors cytoplasmic dynein-1Distinct protein complexesCytoplasmic dynein-1Cryo-electron microscopyProtein Arp1Protein complexesAngstrom structureDynein 1DynactinEssential cofactorΒ-actinDyneinShoulder domainDependent interactionFilamentsComplexesArp1CofactorActinCopiesInteractionPeptidesDomain
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 ResearchCryo-EM structures of two bovine adenovirus type 3 intermediates
Cheng L, Huang X, Li X, Xiong W, Sun W, Yang C, Zhang K, Wang Y, Liu H, Huang X, Ji G, Sun F, Zheng C, Zhu P. Cryo-EM structures of two bovine adenovirus type 3 intermediates. Virology 2014, 450: 174-181. PMID: 24503080, DOI: 10.1016/j.virol.2013.12.012.Peer-Reviewed Original ResearchConceptsCryo-electron tomography analysisDNA encapsidation processCryo-EM structureCryo-electron microscopyVertebrate speciesFirst structural comparisonProtein VIDNA encapsidationEncapsidation processStructural comparisonProtein IXUnique conformationBackbone levelIntermediate structuresHuman ADMass spectrometryLater stagesEncapsidationSpeciesSimilar structureBAd3HostIntermediatesAssemblyCleavage
2013
Identification 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 Relationship
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