2021
CD1a selectively captures endogenous cellular lipids that broadly block T cell response
Cotton R, Wegrecki M, Cheng T, Chen Y, Veerapen N, Le Nours J, Orgill D, Pomahac B, Talbot S, Willis R, Altman J, de Jong A, Van Rhijn I, Clark R, Besra G, Ogg G, Rossjohn J, Moody D. CD1a selectively captures endogenous cellular lipids that broadly block T cell response. Journal Of Experimental Medicine 2021, 218: e20202699. PMID: 33961028, PMCID: PMC8111460, DOI: 10.1084/jem.20202699.Peer-Reviewed Original ResearchConceptsNatural endogenous inhibitorsEndogenous lipidsCD1a proteinCellular lipidsT cell activationMembrane phospholipidsLonger lipidsSurface residuesEndogenous inhibitorLipidomics methodDetailed chemical structureCell activationLipidsCellsNatural blockerSphingolipidsDisplay platformProteinCrystal structureResiduesCell responsesBindingTetramerC42Sphingomyelin
2004
Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch
Dong G, Chakshusmathi G, Wolin SL, Reinisch KM. Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch. The EMBO Journal 2004, 23: 1000-1007. PMID: 14976553, PMCID: PMC380972, DOI: 10.1038/sj.emboj.7600115.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsAutoantigensConserved SequenceCrystallography, X-RayHelix-Turn-Helix MotifsHydroxylationModels, MolecularMolecular Sequence DataMutationPhosphatesProtein BindingProtein Structure, TertiaryRibonucleoproteinsRNASequence AlignmentSubstrate SpecificityTrypanosoma brucei bruceiConceptsLa motifLa proteinRNA polymerase III transcriptsFirst structural insightsRNA-binding proteinPolymerase III transcriptsHelix domainNuclear phosphoproteinRNA substratesMutagenesis experimentsStructural insightsConserved regionsHigh-affinity bindingAromatic patchHelix architectureProteinSurface residuesMotifRNAUridylateCritical roleTranscriptsPhosphoproteinExonucleaseFolding
1992
Different features of the MHC class I heterodimer have evolved at different rates. Chicken B-F and beta 2-microglobulin sequences reveal invariant surface residues.
Kaufman J, Andersen R, Avila D, Engberg J, Lambris J, Salomonsen J, Welinder K, Skjødt K. Different features of the MHC class I heterodimer have evolved at different rates. Chicken B-F and beta 2-microglobulin sequences reveal invariant surface residues. The Journal Of Immunology 1992, 148: 1532-46. PMID: 1538136, DOI: 10.4049/jimmunol.148.5.1532.Peer-Reviewed Original ResearchConceptsPatches of invariant residuesAlpha 3 domainTurkey beta 2mChicken alpha 1Structurally homologous domainsExpressed class I moleculeMHC class I heterodimersSurface residuesAlpha 3Interdomain contact sitesBeta 2 domainClassical class I moleculesAmino acid compositionSmall exonsVertebrate homologsCDNA clonesAllelic residuesInvariant residuesHomology domainCDNA sequenceAlpha 2 domainsClass I moleculesContact sitesCytoplasmic regionExtracellular domain
1991
Using Chicken Class I Sequences to Understand How Xenoantibodies Crossreact with MHC-like Molecules in Nonmammalian Vertebrates1
KAUFMAN J, SALOMONSEN J, RIEGERT P, SKJØDT K. Using Chicken Class I Sequences to Understand How Xenoantibodies Crossreact with MHC-like Molecules in Nonmammalian Vertebrates1. Integrative And Comparative Biology 1991, 31: 570-579. DOI: 10.1093/icb/31.3.570.Peer-Reviewed Original ResearchPatches of invariant residuesContent of guanineRate of evolutionClass I sequencesSurface residuesInterdomain contact sitesInvariant residuesHomology domainEvolutionary historyIntradomain contactsI sequencesContact sitesImmunoglobulin lociMHC-like moleculesNonmammalian vertebratesMHC moleculesMicrochromosomesAmphibiansAntigenic similarityReptilesRabbit antiserumResiduesMammalsChickenInterdomain
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