2022
New vistas unfold: Chicken MHC molecules reveal unexpected ways to present peptides to the immune system
Halabi S, Kaufman J. New vistas unfold: Chicken MHC molecules reveal unexpected ways to present peptides to the immune system. Frontiers In Immunology 2022, 13: 886672. PMID: 35967451, PMCID: PMC9372762, DOI: 10.3389/fimmu.2022.886672.Peer-Reviewed Original ResearchConceptsMajor histocompatibility complexC-terminusPeptide C-terminusNon-mammalian vertebratesStructural studiesCell surface expression levelsMajor histocompatibility complex moleculesPolymorphic TAPClassical class IClass I genesJawed vertebratesAnchor residuesI geneAcid residuesTapasin geneResponse to infectious pathogensSurface expression levelsMolecular explanationDomestic chickensPeptide bindingClass II moleculesHydrophobic pocketAllelesBinding sitesBinding peptides
2019
Human keratin 1/10‐1B tetramer structures reveal a knob‐pocket mechanism in intermediate filament assembly
Eldirany SA, Ho M, Hinbest AJ, Lomakin IB, Bunick CG. Human keratin 1/10‐1B tetramer structures reveal a knob‐pocket mechanism in intermediate filament assembly. The EMBO Journal 2019, 38: embj2018100741. PMID: 31036554, PMCID: PMC6545558, DOI: 10.15252/embj.2018100741.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionCircular DichroismCrystallography, X-RayCytoskeletonDynamic Light ScatteringHumansHydrophobic and Hydrophilic InteractionsIntermediate Filament ProteinsKeratin-1Keratin-10Models, MolecularMutation, MissenseProtein FoldingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondarySkin DiseasesConceptsFilament assemblyN-terminal hydrophobic pocketIntermediate filament assemblyTetramer assemblyÅ structureÅ resolutionCircular dichroism measurementsTetramer formationAssembly mechanismHydrophobic faceHydrophobic pocketSecondary structureOctamer structureEpidermolytic palmoplantar keratodermaKeratin filamentsIntermediate filamentsMutationsPathogenic mutationsTetramer structureDichroism measurementsAtomic resolutionAssemblyBiochemical determinantsKeratin 1/10Tetramer
2015
Crystal Structure of Human Profilaggrin S100 Domain and Identification of Target Proteins Annexin II, Stratifin, and HSP27
Bunick CG, Presland RB, Lawrence OT, Pearton DJ, Milstone LM, Steitz TA. Crystal Structure of Human Profilaggrin S100 Domain and Identification of Target Proteins Annexin II, Stratifin, and HSP27. Journal Of Investigative Dermatology 2015, 135: 1801-1809. PMID: 25760235, PMCID: PMC4466033, DOI: 10.1038/jid.2015.102.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAnnexin A2Biomarkers, TumorCells, CulturedCrystallizationEpidermal CellsEpidermisExoribonucleasesFilaggrin ProteinsHSP27 Heat-Shock ProteinsHumansIntermediate Filament ProteinsKeratinocytesProtein BindingProtein TransportS100 ProteinsSensitivity and SpecificitySpectrometry, FluorescenceConceptsÅ resolution crystal structureProtein-protein interactionsHuman profilaggrinCalcium-binding domainKeratinocyte terminal differentiationMolecular functionsProtein interactionsTerminal domainShock protein 27Cell envelopeIdentification of targetsN-terminusMolecular approachesTerminal differentiationNormal epidermal barrierHydrophobic pocketSpecific functionsAnnexin IIStable dimerMolecular interfaceProtein 27Proteolytic productsProfilaggrinProteinCrystal structure
2010
Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*
Li X, Zhang R, Zhang H, He Y, Ji W, Min W, Boggon TJ. Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*. Journal Of Biological Chemistry 2010, 285: 24099-24107. PMID: 20489202, PMCID: PMC2911348, DOI: 10.1074/jbc.m110.128470.Peer-Reviewed Original ResearchMeSH KeywordsApoptosis Regulatory ProteinsBinding, CompetitiveBrainCrystallography, X-RayDimerizationHemangioma, Cavernous, Central Nervous SystemHumansKineticsMembrane ProteinsMolecular ConformationMutationPaxillinProtein ConformationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProto-Oncogene ProteinsConceptsN-terminal dimerization domainPaxillin LD motifsCerebral cavernous malformationsAlpha-helical proteinsLD motifsCCM complexHomology domainFocal adhesionsDimerization domainMolecular basisHydrophobic pocketHuman populationCCM3 mutationsMutationsCCM3Crystal structureVascular integrityCCM2DomainPaxillinProteinMotifCCM1InteractionCells
2004
NMR-Driven Discovery of Benzoylanthranilic Acid Inhibitors of Far Upstream Element Binding Protein Binding to the Human Oncogene c-myc Promoter
Huth JR, Yu L, Collins I, Mack J, Mendoza R, Isaac B, Braddock DT, Muchmore SW, Comess KM, Fesik SW, Clore GM, Levens D, Hajduk PJ. NMR-Driven Discovery of Benzoylanthranilic Acid Inhibitors of Far Upstream Element Binding Protein Binding to the Human Oncogene c-myc Promoter. Journal Of Medicinal Chemistry 2004, 47: 4851-4857. PMID: 15369388, DOI: 10.1021/jm0497803.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCombinatorial Chemistry TechniquesDNA HelicasesDNA, Single-StrandedDNA-Binding ProteinsDrug DesignGenes, mycHumansInhibitory Concentration 50LigandsMagnetic Resonance SpectroscopyModels, MolecularPromoter Regions, GeneticProtein ConformationProtein Structure, TertiaryProto-Oncogene MasRepetitive Sequences, Amino AcidRNA-Binding ProteinsStructure-Activity RelationshipConceptsUpstream element binding proteinC-myc expressionElement-binding proteinC-Myc pathwayTranscription factorsBinding proteinHost of proteinsRelated transcription factorsAberrant gene expressionC-myc promoterGel shift analysisSlow cell growthC-myc regulationProto-oncogene c-mycFBP bindsKH domainsFBP functionInhibits DNADevelopment of therapeuticsOwn expressionGene expressionHydrophobic pocketC-MycBinding pocketsCell growth
1995
Mechanism of Inhibition of HIV-1 Reverse Transcriptase by Nonnucleoside Inhibitors
Spence R, Kati W, Anderson K, Johnson K. Mechanism of Inhibition of HIV-1 Reverse Transcriptase by Nonnucleoside Inhibitors. Science 1995, 267: 988-993. PMID: 7532321, PMCID: PMC7526747, DOI: 10.1126/science.7532321.Peer-Reviewed Original ResearchConceptsActive site catalytic residuesPre-steady-state kinetic analysisNucleotide-induced conformational changesInterfere with nucleotide bindingPre-steady-state burstEnzyme-DNA complexPre-steady-stateReverse transcriptasePresence of saturating concentrationsCatalytic residuesNucleotide bindingNucleoside triphosphatesDNA polymerizationNucleotide analogsHydrophobic pocketMechanism of inhibitionNonnucleoside inhibitorsConformational changesNoncompetitive inhibitorInhibition of HIV-1 reverse transcriptaseKinetic analysisHIV-1 reverse transcriptaseSaturating concentrationsTranscriptaseInhibitors
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