2024
De novo-designed transmembrane proteins bind and regulate a cytokine receptor
Mravic M, He L, Kratochvil H, Hu H, Nick S, Bai W, Edwards A, Jo H, Wu Y, DiMaio D, DeGrado W. De novo-designed transmembrane proteins bind and regulate a cytokine receptor. Nature Chemical Biology 2024, 20: 751-760. PMID: 38480980, PMCID: PMC11142920, DOI: 10.1038/s41589-024-01562-z.Peer-Reviewed Original ResearchTM proteinsTM regionTarget membrane proteinsComplex biological functionsTM domainTM helicesInteraction partnersTransmembrane proteinsMembrane proteinsReceptor homodimerizationBiological functionsCytokine receptorsBinding topologyAmino acidsProteinErythropoietin receptorHomodimerizationCell proliferationTransmembraneEpoRIn vitroMolecular modelingBinding modeReceptorsMotif
2015
Biologically active LIL proteins built with minimal chemical diversity
Heim EN, Marston JL, Federman RS, Edwards AP, Karabadzhak AG, Petti LM, Engelman DM, DiMaio D. Biologically active LIL proteins built with minimal chemical diversity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: e4717-e4725. PMID: 26261320, PMCID: PMC4553812, DOI: 10.1073/pnas.1514230112.Peer-Reviewed Original ResearchConceptsAmino acidsTransmembrane proteinSpecific biological activityPlatelet-derived growth factor β receptorArtificial transmembrane proteinsChemical diversityGrowth factor β receptorHydrophobic amino acidsLIL proteinsKnown proteinsIndividual amino acidsTransmembrane domainCellular contextDifferent amino acidsComplete mutagenesisMost proteinsBiological activityActive proteinSimple proteinSingle isoleucineSpecific sequencesProteinDiversityLeucineΒ receptor
2000
The platelet-derived growth factor ß receptor as a target of the bovine papillomavirus E5 protein
DiMaio D, Lai C, Mattoon D. The platelet-derived growth factor ß receptor as a target of the bovine papillomavirus E5 protein. Cytokine & Growth Factor Reviews 2000, 11: 283-293. PMID: 10959076, DOI: 10.1016/s1359-6101(00)00012-5.Peer-Reviewed Original ResearchConceptsE5 proteinBovine papillomavirus E5 proteinSH2 domain-containing proteinsCellular signal transduction pathwaysDomain-containing proteinsSignal transduction complexSignal transduction pathwaysLigand-independent fashionGrowth factor receptor activitySpecific transmembraneTransduction complexCytoplasmic domainTransmembrane proteinTransduction pathwaysReceptor dimerizationTyrosine residuesAmino acidsProteinViral transformationDirect interactionBovine papillomavirusUnique mechanismStable complexesComplex formationNew insights
1998
Role of Glutamine 17 of the Bovine Papillomavirus E5 Protein in Platelet-Derived Growth Factor β Receptor Activation and Cell Transformation
Klein O, Polack G, Surti T, Kegler-Ebo D, Smith S, DiMaio D. Role of Glutamine 17 of the Bovine Papillomavirus E5 Protein in Platelet-Derived Growth Factor β Receptor Activation and Cell Transformation. Journal Of Virology 1998, 72: 8921-8932. PMID: 9765437, PMCID: PMC110309, DOI: 10.1128/jvi.72.11.8921-8932.1998.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinPDGF beta receptorE5 proteinTransform cellsCellular platelet-derived growth factor (PDGF) beta receptorAmino acidsBa/F3 hematopoietic cellsPosition 17Cell transformationPlatelet-derived growth factor beta receptorHomodimeric transmembrane proteinReceptor tyrosine phosphorylationGrowth factor beta receptorReceptor tyrosine kinasesPDGF receptor tyrosine kinaseReceptor activationPossible amino acidsBeta receptorsStable complexesComplex formationMutant proteinsTransmembrane domainTransmembrane proteinGrowth factor-beta (TGF-beta) receptor activationTyrosine phosphorylation
1997
Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein
Petti L, Reddy V, Smith S, DiMaio D. Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein. Journal Of Virology 1997, 71: 7318-7327. PMID: 9311809, PMCID: PMC192076, DOI: 10.1128/jvi.71.10.7318-7327.1997.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBovine papillomavirus 1CattleCell LineCell MembraneErbB ReceptorsHumansInterleukin-3KineticsLeucineLysineMiceMolecular Sequence DataMutagenesis, Site-DirectedOncogene Proteins v-sisOncogene Proteins, ViralPoint MutationPolymerase Chain ReactionProtein Structure, SecondaryRatsReceptor, ErbB-2Receptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorReceptors, VirusRecombinant Fusion ProteinsRetroviridae Proteins, OncogenicSequence AlignmentThreonineTransfectionConceptsBovine papillomavirus E5 proteinE5 proteinTransmembrane domainPDGF beta receptorAmino acidsCellular platelet-derived growth factor (PDGF) beta receptorReceptor mutantsJuxtamembrane domainPlatelet-derived growth factor beta receptorPutative transmembrane domainsMurine Ba/F3 cellsCarboxyl-terminal domainBa/F3 cellsV-sisReceptor tyrosine phosphorylationExtracellular juxtamembrane domainGrowth factor beta receptorSpecific amino acidsProductive interactionReceptor activationPlatelet-derived growth factor receptorAcidic amino acidsComplex formationThreonine residuesBeta receptors
1992
The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine
Kulke R, Horwitz B, Zibello T, DiMaio D. The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine. Journal Of Virology 1992, 66: 505-511. PMID: 1727496, PMCID: PMC238311, DOI: 10.1128/jvi.66.1.505-511.1992.Peer-Reviewed Original ResearchConceptsHydrophobic amino acidsAmino acidsE5 proteinRandom hydrophobic sequencesHydrophobic domainRodent fibroblast cell linesCentral hydrophobic domainHydrophobic amino acid sequenceCarboxyl-terminal amino acidsMouse C127 cellsAmino acid sequenceClasses of mutantsAbsence of glutamineBovine papillomavirus E5Mutant proteinsTransforming proteinDefective mutantsHydrophobic sequenceFibroblast cell lineProtein stabilityAcid sequenceC127 cellsHomodimer formationEfficient transformationProtein
1989
Transforming activity of a 16-amino-acid segment of the bovine papillomavirus E5 protein linked to random sequences of hydrophobic amino acids
Horwitz B, Weinstat D, DiMaio D. Transforming activity of a 16-amino-acid segment of the bovine papillomavirus E5 protein linked to random sequences of hydrophobic amino acids. Journal Of Virology 1989, 63: 4515-4519. PMID: 2552136, PMCID: PMC251082, DOI: 10.1128/jvi.63.11.4515-4519.1989.Peer-Reviewed Original ResearchConceptsE5 proteinAmino acidsWild-type E5 proteinBovine papillomavirus E5 proteinAmino acid sequence requirementsHydrophobic amino acid sequenceCarboxyl-terminal amino acidsMouse C127 cellsAmino acid sequenceBovine papillomavirus type 1Carboxyl-terminal portionWild-type onesHydrophobic amino acidsPapillomavirus type 1Hydrophobic sequenceDifferent amino acidsAcid sequenceC127 cellsSequence requirementsE5 geneCell transformationFoci formationSubstitution mutationsCell membraneProtein
1988
44-Amino-Acid E5 Transforming Protein of Bovine Papillomavirus Requires a Hydrophobic Core and Specific Carboxyl-Terminal Amino Acids
Horwitz B, Burkhardt A, Schlegel R, DiMaio D. 44-Amino-Acid E5 Transforming Protein of Bovine Papillomavirus Requires a Hydrophobic Core and Specific Carboxyl-Terminal Amino Acids. Molecular And Cellular Biology 1988, 8: 4071-4078. DOI: 10.1128/mcb.8.10.4071-4078.1988.Peer-Reviewed Original ResearchAmino acid substitutionsE5 proteinAmino acidsTransforming proteinAcid substitutionsCarboxyl-terminal thirdCarboxyl-terminal amino acidsCharacterization of mutantsSpecific amino acid sequencesMouse C127 cellsAmino acid sequenceBovine papillomavirus type 1Specific amino acidsHydrophobic amino acidsPapillomavirus type 1Focus-forming activityCysteine residuesAcid sequenceC127 cellsSaturation mutagenesisE5 geneTransforming activityEssential amino acidsFoci formationMissense mutations44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids.
Horwitz B, Burkhardt A, Schlegel R, DiMaio D. 44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids. Molecular And Cellular Biology 1988, 8: 4071-4078. PMID: 2847028, PMCID: PMC365476, DOI: 10.1128/mcb.8.10.4071.Peer-Reviewed Original ResearchConceptsAmino acid substitutionsE5 proteinAmino acidsTransforming proteinAcid substitutionsCarboxyl-terminal thirdCarboxyl-terminal amino acidsCharacterization of mutantsSpecific amino acid sequencesMouse C127 cellsAmino acid sequenceBovine papillomavirus type 1Specific amino acidsHydrophobic amino acidsPapillomavirus type 1Focus-forming activityCysteine residuesAcid sequenceC127 cellsSaturation mutagenesisE5 geneTransforming activityEssential amino acidsFoci formationMissense mutations