2025
Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions
Robles J, Stiegler A, Boggon T, Turk B. Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions. Journal Of Biological Chemistry 2025, 301: 108348. PMID: 40015635, PMCID: PMC11982978, DOI: 10.1016/j.jbc.2025.108348.Peer-Reviewed Original ResearchShort linear motifsCancer hotspot mutationsLinear motifsERK substratesYeast two-hybrid libraryHotspot mutationsTwo-hybrid libraryCancer-associated mutantsDocking interactionsWild-type ERK2Cancer-associated mutationsDocking motifBinding sequenceKinase ERK2Co-crystal structureMutant formsERK2 mutantsDisordered regionsERK2MotifStructural rationalePeptide bindingMutationsWT kinasePeptide fragmentsStructural basis of promiscuous inhibition of Listeria virulence activator PrfA by oligopeptides
Hainzl T, Scortti M, Lindgren C, Grundström C, Krypotou E, Vázquez-Boland J, Sauer-Eriksson A. Structural basis of promiscuous inhibition of Listeria virulence activator PrfA by oligopeptides. Cell Reports 2025, 44: 115290. PMID: 39970044, DOI: 10.1016/j.celrep.2025.115290.Peer-Reviewed Original ResearchConceptsDNA-binding helix-turn-helix motifInhibit virulence gene expressionVirulence gene expressionPathogen Listeria monocytogenesPrfA activityVirulence factorsPrfAMaster regulatorsHydrophobic residuesInhibitory bindingGene expressionStructural basisBinding promiscuityPeptide bindingBinding sitesConformational changesPeptide residuesOligopeptidesPeptideInhibitory peptidesBindingPeptide backboneResiduesPromiscuous inhibitionExpression
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
2018
Unfinished Business: Evolution of the MHC and the Adaptive Immune System of Jawed Vertebrates
Kaufman J. Unfinished Business: Evolution of the MHC and the Adaptive Immune System of Jawed Vertebrates. Annual Review Of Immunology 2018, 36: 383-409. PMID: 29677478, DOI: 10.1146/annurev-immunol-051116-052450.Peer-Reviewed Original ResearchConceptsJawed vertebratesAdaptive immune system of jawed vertebratesImmune system of jawed vertebratesII genesGenome-wide duplicationAdaptive immune systemClassical class IInnate immune responseGenetic regionsGene linkageGenesPeptide bindingAntigen-specific receptorsVertebratesAdaptive immunityClass IPotential importanceImmune systemImmune responseMHCMHC moleculesCoevolution
2013
Insights on the Facet Specific Adsorption of Amino Acids and Peptides toward Platinum
Ramakrishnan SK, Martin M, Cloitre T, Firlej L, Cuisinier F, Gergely C. Insights on the Facet Specific Adsorption of Amino Acids and Peptides toward Platinum. Journal Of Chemical Information And Modeling 2013, 53: 3273-3279. PMID: 24289530, DOI: 10.1021/ci400630d.Peer-Reviewed Original ResearchConceptsMolecular dynamics simulationsInorganic surfacesPt facetsSpecific adsorptionPredictable conformationsNovel nanomaterialsInorganic materialsDifferential adsorptionAdhesion peptidesMolecular architectureDynamics simulationsAdsorptionProgrammable shapesRecognition behaviorBuilding blocksAmino acidsEnhanced affinityPeptide bindingPolar amino acidsCrystallographic planesAcidPeptidesBiomoleculesBionanomaterialsNanomaterials
2011
The dominantly expressed class I molecule of the chicken MHC is explained by coevolution with the polymorphic peptide transporter (TAP) genes
Walker B, Hunt L, Sowa A, Skjødt K, Göbel T, Lehner P, Kaufman J. The dominantly expressed class I molecule of the chicken MHC is explained by coevolution with the polymorphic peptide transporter (TAP) genes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 8396-8401. PMID: 21536896, PMCID: PMC3100931, DOI: 10.1073/pnas.1019496108.Peer-Reviewed Original ResearchConceptsExpressed class I moleculeChicken MHC haplotypesTransporter associated with antigen presentationModerate sequence diversityMHC haplotypesClass I genesClass I moleculesSequence diversityPrimordial MHCI genePeptide motifsChicken MHCChicken linesAllelic polymorphismI moleculesPeptide translocationPeptide bindingAdaptive immune systemMHC associationsCoevolutionPeptide transportHaplotypesAntigen presentation pathwayPeptide positionChicken
2007
Structures of an MHC Class I Molecule from B21 Chickens Illustrate Promiscuous Peptide Binding
Koch M, Camp S, Collen T, Avila D, Salomonsen J, Wallny H, van Hateren A, Hunt L, Jacob J, Johnston F, Marston D, Shaw I, Dunbar P, Cerundolo V, Jones E, Kaufman J. Structures of an MHC Class I Molecule from B21 Chickens Illustrate Promiscuous Peptide Binding. Immunity 2007, 27: 885-899. PMID: 18083574, DOI: 10.1016/j.immuni.2007.11.007.Peer-Reviewed Original ResearchConceptsMajor histocompatibility complexB21 haplotypeChicken major histocompatibility complexBF2*2101Peptide-binding siteMajor histocompatibility complex class I moleculesClass I moleculesBinding grooveGenetic associationStructure of major histocompatibility complexPromiscuous bindingPeptide bindingI moleculesHaplotypesCharge-transfer systemsMajor histocompatibility complex moleculesConformational flexibilityCentral cavityInfectious pathogensHistocompatibility complexAnchor residuesBindingOncogenic herpesvirusPeptideResidues
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