2016
Mechanism of substrate specificity of phosphatidylinositol phosphate kinases
Muftuoglu Y, Xue Y, Gao X, Wu D, Ha Y. Mechanism of substrate specificity of phosphatidylinositol phosphate kinases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 8711-8716. PMID: 27439870, PMCID: PMC4978281, DOI: 10.1073/pnas.1522112113.Peer-Reviewed Original ResearchConceptsPhosphatidylinositol phosphate kinaseKinase familySubstrate specificityPhosphate kinasePhosphatidylinositol phosphate kinase (PIPK) familyZebrafish type IMembrane trafficking processesExquisite substrate specificityType III kinaseEukaryotic cellsInositol ringPhosphorylation resultsSubstrate recognitionTrafficking processesSpecificity loopPhosphatidylinositol derivativesBiological functionsPhosphatidylinositol 4PhosphatidylinositolKinaseStructural motifsType IBisphosphateLoop functionsComplex patterns
2011
Crystal structure of amyloid precursor-like protein 1 and heparin complex suggests a dual role of heparin in E2 dimerization
Xue Y, Lee S, Ha Y. Crystal structure of amyloid precursor-like protein 1 and heparin complex suggests a dual role of heparin in E2 dimerization. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 16229-16234. PMID: 21930949, PMCID: PMC3182750, DOI: 10.1073/pnas.1103407108.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid beta-Protein PrecursorCrystallography, X-RayDimerizationHeparinModels, MolecularProtein BindingProtein ConformationThe crystal structure of GXGD membrane protease FlaK
Hu J, Xue Y, Lee S, Ha Y. The crystal structure of GXGD membrane protease FlaK. Nature 2011, 475: 528-531. PMID: 21765428, PMCID: PMC3894692, DOI: 10.1038/nature10218.Peer-Reviewed Original ResearchConceptsFamily of proteasesFirst crystal structureIntramembrane proteasesPrepilin peptidaseMethanococcus maripaludisMembrane proteasePreflagellin peptidaseFamilial Alzheimer's diseaseVirulence factorsAspartyl proteaseBiochemical analysisProteasePathogenic bacteriaStructural knowledgePresenilinPeptidaseCrystal structureSoluble counterpartActive siteFamilyRational designAspartylBacteriaAlzheimer's diseaseFundamental differences
2006
Crystal structure of a rhomboid family intramembrane protease
Wang Y, Zhang Y, Ha Y. Crystal structure of a rhomboid family intramembrane protease. Nature 2006, 444: 179-180. PMID: 17051161, DOI: 10.1038/nature05255.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsBinding SitesCatalysisCell MembraneCrystallizationCrystallography, X-RayDNA-Binding ProteinsEndopeptidasesEscherichia coliEscherichia coli ProteinsHydrophobic and Hydrophilic InteractionsMembrane ProteinsModels, MolecularProtein Structure, TertiarySubstrate SpecificityWaterConceptsMembrane proteinsEscherichia coli GlpGÅ resolution crystal structureSite-2 proteaseIntegral membrane proteinsPutative active siteResolution crystal structureHydrophilic active siteRhomboid proteasesIntramembrane proteasesIntramembrane proteolysisTransmembrane segmentsTransmembrane domainActive siteProtease familyMembrane bilayerProtein interiorCore domainGating mechanismGlpGΓ-secretaseHydrophobic environmentCrystal structureProteaseLoop structure
2004
The X-Ray Structure of an Antiparallel Dimer of the Human Amyloid Precursor Protein E2 Domain
Wang Y, Ha Y. The X-Ray Structure of an Antiparallel Dimer of the Human Amyloid Precursor Protein E2 Domain. Molecular Cell 2004, 15: 343-353. PMID: 15304215, DOI: 10.1016/j.molcel.2004.06.037.Peer-Reviewed Original ResearchConceptsMembrane protein precursorsX-ray structureSpectrin familyHeparan sulfate proteoglycanDimer interfaceBiological functionsStructure of E2Protein structureProtein precursorPutative ligandE2 domainContinuous helixExtracellular matrixUnexpected resemblanceAntiparallel dimerSulfate proteoglycanAntiparallel orientationPrecursor presentDomainBindsHelixDimerizationSecond monomerH1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes
Russell R, Gamblin S, Haire L, Stevens D, Xiao B, Ha Y, Skehel J. H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes. Virology 2004, 325: 287-296. PMID: 15246268, DOI: 10.1016/j.virol.2004.04.040.Peer-Reviewed Original ResearchThe Structure and Receptor Binding Properties of the 1918 Influenza Hemagglutinin
Gamblin S, Haire L, Russell R, Stevens D, Xiao B, Ha Y, Vasisht N, Steinhauer D, Daniels R, Elliot A, Wiley D, Skehel J. The Structure and Receptor Binding Properties of the 1918 Influenza Hemagglutinin. Science 2004, 303: 1838-1842. PMID: 14764886, DOI: 10.1126/science.1093155.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesBirdsCrystallography, X-RayHemagglutinin Glycoproteins, Influenza VirusHistory, 20th CenturyHumansHydrogen BondingInfluenza A virusInfluenza, HumanMembrane GlycoproteinsModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, TertiaryReceptors, VirusSequence AlignmentSialic AcidsSpecies SpecificitySwine
2001
X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs
Ha Y, Stevens D, Skehel J, Wiley D. X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 11181-11186. PMID: 11562490, PMCID: PMC58807, DOI: 10.1073/pnas.201401198.Peer-Reviewed Original Research