2021
Structural basis for ligand reception by anaplastic lymphoma kinase
Li T, Stayrook SE, Tsutsui Y, Zhang J, Wang Y, Li H, Proffitt A, Krimmer SG, Ahmed M, Belliveau O, Walker IX, Mudumbi KC, Suzuki Y, Lax I, Alvarado D, Lemmon MA, Schlessinger J, Klein DE. Structural basis for ligand reception by anaplastic lymphoma kinase. Nature 2021, 600: 148-152. PMID: 34819665, PMCID: PMC8639777, DOI: 10.1038/s41586-021-04141-7.Peer-Reviewed Original Research
2020
Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases
Sheetz JB, Mathea S, Karvonen H, Malhotra K, Chatterjee D, Niininen W, Perttilä R, Preuss F, Suresh K, Stayrook SE, Tsutsui Y, Radhakrishnan R, Ungureanu D, Knapp S, Lemmon MA. Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases. Molecular Cell 2020, 79: 390-405.e7. PMID: 32619402, PMCID: PMC7543951, DOI: 10.1016/j.molcel.2020.06.018.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBaculoviridaeBinding SitesCell Adhesion MoleculesCell LineCloning, MolecularCrystallography, X-RayGene ExpressionHumansMiceModels, MolecularPrecursor Cells, B-LymphoidProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein Kinase InhibitorsReceptor Protein-Tyrosine KinasesReceptor Tyrosine Kinase-like Orphan ReceptorsReceptors, Eph FamilyRecombinant ProteinsSf9 CellsSmall Molecule LibrariesSpodopteraStructural Homology, ProteinSubstrate SpecificityConceptsInsulin receptor kinasePseudokinase domainReceptor tyrosine kinasesTyrosine kinaseNon-catalytic functionsATP-binding pocketType II inhibitorsDomain plasticityActivation loopReceptor kinaseInactive conformationStructural insightsPseudokinasesATP siteStructural comparisonAromatic residuesKinaseAlternative interactionsApparent lackImportant roleDomainWntMotifROR1Residues
2018
Combination of aptamer and drug for reversible anticoagulation in cardiopulmonary bypass
Gunaratne R, Kumar S, Frederiksen J, Stayrook S, Lohrmann J, Perry K, Bompiani K, Chabata C, Thalji N, Ho M, Arepally G, Camire R, Krishnaswamy S, Sullenger B. Combination of aptamer and drug for reversible anticoagulation in cardiopulmonary bypass. Nature Biotechnology 2018, 36: 606-613. PMID: 29863725, PMCID: PMC6349032, DOI: 10.1038/nbt.4153.Peer-Reviewed Original Research
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 activatorReceptorsSequestrationProteinActivatorLigandsSpitzTGFTherapeuticsDomainCrystal structure of the λ repressor and a model for pairwise cooperative operator binding
Stayrook S, Jaru-Ampornpan P, Ni J, Hochschild A, Lewis M. Crystal structure of the λ repressor and a model for pairwise cooperative operator binding. Nature 2008, 452: 1022-1025. PMID: 18432246, DOI: 10.1038/nature06831.Peer-Reviewed Original ResearchStructural basis for the function and inhibition of an influenza virus proton channel
Stouffer A, Acharya R, Salom D, Levine A, Di Costanzo L, Soto C, Tereshko V, Nanda V, Stayrook S, DeGrado W. Structural basis for the function and inhibition of an influenza virus proton channel. Nature 2008, 451: 596-599. PMID: 18235504, PMCID: PMC3889492, DOI: 10.1038/nature06528.Peer-Reviewed Original Research
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 Structure of a Designed Diiron(III) Protein: Implications for Cofactor Stabilization and Catalysis
Wade H, Stayrook S, DeGrado W. The Structure of a Designed Diiron(III) Protein: Implications for Cofactor Stabilization and Catalysis. Angewandte Chemie International Edition 2006, 45: 4951-4954. PMID: 16819737, DOI: 10.1002/anie.200600042.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCatalysisCoenzymesCrystallography, X-RayIronMixed Function OxygenasesMolecular StructureOxidation-ReductionOxygenasesRibonucleotide ReductasesThe 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
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-rayHeptadAnalysis and Design of Turns in α-Helical Hairpins
Lahr S, Engel D, Stayrook S, Maglio O, North B, Geremia S, Lombardi A, DeGrado W. Analysis and Design of Turns in α-Helical Hairpins. Journal Of Molecular Biology 2005, 346: 1441-1454. PMID: 15713492, DOI: 10.1016/j.jmb.2004.12.016.Peer-Reviewed Original Research
2003
X-ray Structure of a Maquette Scaffold
Huang S, Gibney B, Stayrook S, Dutton P, Lewis M. X-ray Structure of a Maquette Scaffold. Journal Of Molecular Biology 2003, 326: 1219-1225. PMID: 12589764, DOI: 10.1016/s0022-2836(02)01441-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCrystallography, X-RayModels, MolecularPeptidesProtein Structure, SecondaryConceptsLeft-handed coiled-coilsCoiled-coilAnti-parallel four-helix bundleHeptad repeat patternFour-alpha-helical bundleMaquette scaffoldFour-helix bundleHeme-binding propertiesX-ray structureMAD phasingHeme binding pocketIdentical helicesResidue positionsHeptad repeatHydrophobic residuesPacking interfaceProtein scaffoldEngineering criteriaHeptadMaquettesRepeat patternHelixDesign criteriaX-rayInitial design
2001
Crystal Structure of Human Type III 3α-Hydroxysteroid Dehydrogenase/Bile Acid Binding Protein Complexed with NADP+ and Ursodeoxycholate † , ‡
Jin Y, Stayrook S, Albert R, Palackal N, Penning T, Lewis M. Crystal Structure of Human Type III 3α-Hydroxysteroid Dehydrogenase/Bile Acid Binding Protein Complexed with NADP+ and Ursodeoxycholate † , ‡. Biochemistry 2001, 40: 10161-10168. PMID: 11513593, DOI: 10.1021/bi010919a.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationAllosteric SiteAmino Acid SequenceBinding SitesCloning, MolecularComputer SimulationCrystallography, X-RayEscherichia coliFluoxetineHumansHydroxysteroid DehydrogenasesModels, MolecularMolecular ConformationMolecular Sequence DataNADPProtein BindingProtein Structure, SecondaryRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidUrsodeoxycholic AcidConceptsRat 3alpha-HSDAldo-keto reductase superfamilyBinding protein complexSteroid binding pocketAlpha/beta barrelBound NADP(+Human typeProtein complexesThree-dimensional structureOxyanion holeAndrogen 5alpha-dihydrotestosteroneBinding proteinStructural basisTransport of bile acidsAKR1C2Ternary complexRat isoformsNADP(+SuperfamilyExtended conformationProstatic productionActive siteIsoformsCrystal structureBile acids