2001
Genetic selection for and molecular dynamic modeling of a protein transmembrane domain multimerization motif from a random Escherichia coli genomic library 1 1 Edited by G. von Heijne
Leeds J, Boyd D, Huber D, Sonoda G, Luu H, Engelman D, Beckwith J. Genetic selection for and molecular dynamic modeling of a protein transmembrane domain multimerization motif from a random Escherichia coli genomic library 1 1 Edited by G. von Heijne. Journal Of Molecular Biology 2001, 313: 181-195. PMID: 11601855, DOI: 10.1006/jmbi.2001.5007.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionBacteriophage lambdaBase SequenceBinding SitesCell MembraneCloning, MolecularDimerizationDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGenes, BacterialGenetic VectorsGenomic LibraryMembrane ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein Sorting SignalsProtein Structure, QuaternaryProtein Structure, TertiaryProtein SubunitsProtein TransportRecombinant Fusion ProteinsRepressor ProteinsViral ProteinsViral Regulatory and Accessory ProteinsConceptsTransmembrane domainTransmembrane helix-helix associationE. coli inner membraneMembrane protein structuresGenomic DNA fragmentsHelix-helix associationG. von HeijneHelix-helix interactionsSite-directed mutagenesisSixth transmembrane domainTransmembrane helicesRepressor DNAGenetic toolsInner membraneVon HeijneProtein structureDNA fragmentsGenetic selectionNovel sequencesMultimerization motifMotifSequenceHomomultimerizationDomainMutagenesis
1998
Structure-based prediction of the stability of transmembrane helix–helix interactions: The sequence dependence of glycophorin A dimerization
MacKenzie K, Engelman D. Structure-based prediction of the stability of transmembrane helix–helix interactions: The sequence dependence of glycophorin A dimerization. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 3583-3590. PMID: 9520409, PMCID: PMC19879, DOI: 10.1073/pnas.95.7.3583.Peer-Reviewed Original ResearchConceptsHelix-helix interactionsTransmembrane helix-helix associationTransmembrane helix-helix interactionsHelix-helix associationSingle-point mutantsStructure-based predictionTransmembrane domainMembrane proteinsDimer interfaceDimerization propensitySide-chain hydrophobicityDimer stabilityPoint mutationsSteric clashesMultiple mutationsMutationsSequence dependenceCompensatory effectFavorable van der Waals interactionsMutantsFoldingProteinInteractionDimerizationGlycophorin
1992
Intramembrane Helix-Helix Association in Oligomerization and Transmembrane Signaling
Bormann B, Engelman D. Intramembrane Helix-Helix Association in Oligomerization and Transmembrane Signaling. Annual Review Of Biophysics 1992, 21: 223-242. PMID: 1326354, DOI: 10.1146/annurev.bb.21.060192.001255.Peer-Reviewed Original ResearchConceptsProtein foldingTransmembrane regionReceptor proteinClose contact sitesSignal transductionQuaternary structureReceptor moleculesConformational changesHelical transmembrane regionsAllosteric conformational changeHelix-helix associationConformational change modelTertiary/quaternary structureTransmembrane helicesTransmembrane domainMechanism of insertionCytoplasmic domainTransmembrane signalingContact sitesPrimary structureSecondary structureProteinOligomerizationFoldingProteolytic fragments