2020
Structural elucidation of the cis-prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation
Edani BH, Grabińska KA, Zhang R, Park EJ, Siciliano B, Surmacz L, Ha Y, Sessa WC. Structural elucidation of the cis-prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 20794-20802. PMID: 32817466, PMCID: PMC7456142, DOI: 10.1073/pnas.2008381117.Peer-Reviewed Original ResearchConceptsActive site tunnelProtein glycosylationAtomic resolution structuresGlycosyl carrier lipidsΑ3 helixEnzyme active sitePTase activityResolution structureActive siteEndoplasmic reticulumHomodimeric formCarrier lipidRate-limiting stepGlycosylationCrystal structureDHDDSStructural elucidationPTaseIsoprene chainPrenyltransferaseUnique insightsComplexesUnfavorable stateNgBRHomodimeric
2004
H1 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 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 monomerThe 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