2009
N-terminal Domains Elicit Formation of Functional Pmel17 Amyloid Fibrils*
Watt B, van Niel G, Fowler DM, Hurbain I, Luk KC, Stayrook SE, Lemmon MA, Raposo G, Shorter J, Kelly JW, Marks MS. N-terminal Domains Elicit Formation of Functional Pmel17 Amyloid Fibrils*. Journal Of Biological Chemistry 2009, 284: 35543-35555. PMID: 19840945, PMCID: PMC2790984, DOI: 10.1074/jbc.m109.047449.Peer-Reviewed Original ResearchMeSH KeywordsAmyloidGp100 Melanoma AntigenHeLa CellsHumansMelanosomesMembrane GlycoproteinsProtein FoldingProtein Structure, TertiaryProtein TransportRecombinant ProteinsStructural Homology, ProteinConceptsFibril formationFormation of melanosomesMultivesicular compartmentsImperfect repeatsRPT domainTransmembrane proteinMelanosome maturationTerminal domainIntracellular traffickingMultivesicular bodiesAmyloid foldPrecursor organellesAmyloid-like fibrilsDownstream domainSubcellular organellesAmyloid conversionRegulatory rolePmel17RepeatsEarly stepsStructural coreAmyloid formationProteolytic fragmentsRecombinant fragmentsOrganelles
2008
Structural basis for EGFR ligand sequestration by Argos
Klein DE, Stayrook SE, Shi F, Narayan K, Lemmon MA. Structural basis for EGFR ligand sequestration by Argos. Nature 2008, 453: 1271-1275. PMID: 18500331, PMCID: PMC2526102, DOI: 10.1038/nature06978.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCell LineCrystallography, X-RayDrosophila melanogasterDrosophila ProteinsEpidermal Growth FactorErbB ReceptorsEye ProteinsHumansLigandsMembrane ProteinsModels, MolecularNerve Tissue ProteinsProtein Structure, TertiaryReceptors, Transforming Growth Factor betaSpodopteraConceptsEpidermal growth factor receptorLigand sequestrationEGFR ligand SpitzLigand SpitzMammalian counterpartsGrowth factor receptorStructural basisUrokinase plasminogen activatorStructural homologuesEGFR ligandsFactor receptorAnticancer therapeuticsStructural resemblanceHomologuesPlasminogen activatorReceptorsSequestrationProteinActivatorLigandsSpitzTGFTherapeuticsDomain
2007
Structural Analysis of Lac Repressor Bound to Allosteric Effectors
Daber R, Stayrook S, Rosenberg A, Lewis M. Structural Analysis of Lac Repressor Bound to Allosteric Effectors. Journal Of Molecular Biology 2007, 370: 609-619. PMID: 17543986, PMCID: PMC2715899, DOI: 10.1016/j.jmb.2007.04.028.Peer-Reviewed Original ResearchConceptsHydrogen bond networkHydrogen bondsExtensive hydrogen-bonding networkWater-mediated hydrogen bond networkSugar ringBond networkCrystal structureHydroxyl groupsAllosteric transitionEffector moleculesAnti-inducerSmall moleculesAtomic detailMoleculesStructural conformationC-terminal sub-domainBondsApo-repressorHydrogenHydroxylRepressor functionLac operonLac repressorN-terminalRepressor
2006
The Structural Basis of Cooperative Regulation at an Alternate Genetic Switch
Pinkett H, Shearwin K, Stayrook S, Dodd I, Burr T, Hochschild A, Egan J, Lewis M. The Structural Basis of Cooperative Regulation at an Alternate Genetic Switch. Molecular Cell 2006, 21: 605-615. PMID: 16507359, DOI: 10.1016/j.molcel.2006.01.019.Peer-Reviewed Original ResearchConceptsGenetic switchC-terminal domainTemperate bacteriophagesCooperativity mutantsBacteriophage lambdaGene regulationRegulatory regionsRepressor monomersGenetic screeningGenetic studiesMolecular basisRepressorStructural basisRegulatory activityBacteriophageCooperative regulationRegulationLambdaMutantsGenesTemperate