2001
Polar residues drive association of polyleucine transmembrane helices
Zhou F, Merianos H, Brunger A, Engelman D. Polar residues drive association of polyleucine transmembrane helices. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 2250-2255. PMID: 11226225, PMCID: PMC30124, DOI: 10.1073/pnas.041593698.Peer-Reviewed Original ResearchConceptsPolar residuesPolyleucine sequenceHelix associationTransmembrane helix associationInterhelical hydrogen bondingTransmembrane protein functionTransmembrane helicesForm homoProtein functionTransmembrane proteinDrive associationMembrane proteinsDetergent micellesAsparagine residuesGeneral structural featuresBiological membranesResiduesOligomerization specificityProteinSequenceHelixStructural flexibilitySuch interactionsStructural featuresHeterooligomers
2000
Interhelical hydrogen bonding drives strong interactions in membrane proteins
Xiao Zhou F, Cocco M, Russ W, Brunger A, Engelman D. Interhelical hydrogen bonding drives strong interactions in membrane proteins. Nature Structural & Molecular Biology 2000, 7: 154-160. PMID: 10655619, DOI: 10.1038/72430.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAsparagineCell MembraneChloramphenicol O-AcetyltransferaseCircular DichroismDetergentsDimerizationDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelFungal ProteinsGlycophorinsHydrogen BondingLeucine ZippersMagnetic Resonance SpectroscopyMembrane ProteinsMicellesMicrococcal NucleaseMolecular Sequence DataPeptidesProtein ConformationProtein KinasesProtein Structure, SecondaryRecombinant ProteinsSaccharomyces cerevisiae ProteinsConceptsMembrane proteinsHelix associationTransmembrane α-helicesIntegral membrane proteinsInterhelical hydrogen bondingModel transmembrane helixTransmembrane helicesMembrane helicesGCN4 leucine zipperLeucine zipperPolar residuesSoluble proteinHydrophobic leucineΑ-helixBiological membranesProteinHelixNon-specific interactionsValine (HAV) sequenceMembraneZipperFoldingMotifAsparagineResidues
1999
The Length of the Flexible SNAREpin Juxtamembrane Region Is a Critical Determinant of SNARE-Dependent Fusion
McNew J, Weber T, Engelman D, Söllner T, Rothman J. The Length of the Flexible SNAREpin Juxtamembrane Region Is a Critical Determinant of SNARE-Dependent Fusion. Molecular Cell 1999, 4: 415-421. PMID: 10518222, DOI: 10.1016/s1097-2765(00)80343-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, SurfaceCarrier ProteinsMembrane FusionMembrane ProteinsMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsPliabilityProlineProtein Structure, SecondaryRecombinant ProteinsR-SNARE ProteinsSNARE ProteinsSynaptosomal-Associated Protein 25Syntaxin 1Vesicular Transport ProteinsConceptsJuxtamembrane regionMembrane fusionSNARE-dependent membrane fusionSNARE-dependent fusionHelix-breaking proline residueSNARE proteinsTransmembrane domainSyntaxin 1ACoil domainProline residuesFlexible linkerLipid bilayersCritical determinantFusion efficiencyFusionVAMPDomainProteinRate of fusionSnareVesiclesResiduesLinkerSame changesRegion
1996
Mapping the lipid-exposed surfaces of membrane proteins
Arkin I, MacKenzie K, Fisher L, Aimoto S, Engelman D, Smith S. Mapping the lipid-exposed surfaces of membrane proteins. Nature Structural & Molecular Biology 1996, 3: 240-243. PMID: 8605625, DOI: 10.1038/nsb0396-240.Peer-Reviewed Original ResearchConceptsMembrane proteinsLong transmembrane helixLipid-exposed surfaceThree-dimensional foldHigh-resolution structuresRelative rotational orientationTransmembrane helicesTransmembrane segmentsThird cysteineCysteine residuesLipid environmentHelix interfacePentameric complexProteinLipid interfaceStable complexesHelixResiduesUndergoes exchangeSulphydryl groupsPhospholambanComplexesInternal faceCysteineRotational orientation
1995
Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
Adams P, Arkin I, Engelman D, Brünger A. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nature Structural & Molecular Biology 1995, 2: 154-162. PMID: 7749920, DOI: 10.1038/nsb0295-154.Peer-Reviewed Original ResearchConceptsPentameric ion channelsTransmembrane domainThree-dimensional structureMembrane proteinsHydrophobic residuesΑ-helixIon channelsComputational searchingEnvironmental constraintsTwo-bodyGlobal searchPhospholambanMutagenesisComputational methodsHomopentamerProteinExperimental dataResiduesData yields