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
2005
X-ray Structure of a Water-soluble Analog of the Membrane Protein Phospholamban: Sequence Determinants Defining the Topology of Tetrameric and Pentameric Coiled Coils
Slovic A, Stayrook S, North B, DeGrado W. X-ray Structure of a Water-soluble Analog of the Membrane Protein Phospholamban: Sequence Determinants Defining the Topology of Tetrameric and Pentameric Coiled Coils. Journal Of Molecular Biology 2005, 348: 777-787. PMID: 15826670, DOI: 10.1016/j.jmb.2005.02.040.Peer-Reviewed Original ResearchConceptsHeptad sequence repeatSequence repeatWater-soluble variantCoiled-coilSequence determinationTransmembrane proteinsTruncated constructsPentameric transmembrane proteinsReticulum membraneStable tetramersTetrameric structureLeu residuesCrystal structurePentameric formX-ray structureInterfacial hydrogen bondsProteinHydrogen bondsResiduesRepeatsMembrane protein phospholambanGCN4Water-soluble analogX-rayHeptad
1998
Steroidogenic Acute Regulatory Protein (StAR) Is A Sterol Transfer Protein*
Kallen C, Billheimer J, Summers S, Stayrook S, Lewis M, Strauss J. Steroidogenic Acute Regulatory Protein (StAR) Is A Sterol Transfer Protein*. Journal Of Biological Chemistry 1998, 273: 26285-26288. PMID: 9756854, DOI: 10.1074/jbc.273.41.26285.Peer-Reviewed Original ResearchConceptsSterol carrier protein-2Steroidogenic acute regulatory proteinStAR proteinRegulatory proteinsSterol transferCholesterol side-chain cleavage enzyme systemMitochondrial targeting sequenceSterol transfer activityTransfer proteinSterol transfer proteinsOuter mitochondrial membraneTrypsin-treated mitochondriaAmino acid residuesLipid transfer proteinsTransfer of cholesterolDonor membranesSubstrate cholesterolInner membraneMitochondrial membraneIsolated mitochondriaTarget sequenceN-terminalTemperature-dependent mannerAcid residuesPhosphatidylcholine transferThe Mechanism of Action of Steroidogenic Acute Regulatory Protein (StAR) StAR ACTS ON THE OUTSIDE OF MITOCHONDRIA TO STIMULATE STEROIDOGENESIS*
Arakane F, Kallen C, Watari H, Foster J, Sepuri N, Pain D, Stayrook S, Lewis M, Gerton G, Strauss J. The Mechanism of Action of Steroidogenic Acute Regulatory Protein (StAR) StAR ACTS ON THE OUTSIDE OF MITOCHONDRIA TO STIMULATE STEROIDOGENESIS*. Journal Of Biological Chemistry 1998, 273: 16339-16345. PMID: 9632696, DOI: 10.1074/jbc.273.26.16339.Peer-Reviewed Original ResearchConceptsCOS-1 cellsMitochondrial targeting sequenceWild-type StARSteroidogenic acute regulatory proteinStAR preproteinHis-tagMitochondrial membraneIsolated mitochondriaNH2-terminal mitochondrial targeting sequenceCOS-1Target sequenceRegulatory proteinsMechanism of StAR's actionIn vitro import assayStAR proteinStAR's actionCytoplasm of transfected COS-1 cellsProteins associated with mitochondriaCholesterol side-chain cleavage systemLipoid congenital adrenal hyperplasiaSide-chain cleavage systemLocalized to mitochondriaN-62 StARHis-tagged proteinsAbsence of cytosol