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
2014
X-Ray Structure of an Anticoagulant RNA Aptamer Bound to Factor Xa. Structural Basis for Its Ability to Disrupt Interactions Between Xa and Va within Prothrombinase
Kumar S, Sullenger B, Stayrook S, Krishnaswamy S. X-Ray Structure of an Anticoagulant RNA Aptamer Bound to Factor Xa. Structural Basis for Its Ability to Disrupt Interactions Between Xa and Va within Prothrombinase. Blood 2014, 124: 4232. DOI: 10.1182/blood.v124.21.4232.4232.Peer-Reviewed Original ResearchRNA aptamersC-terminusBinding to factor VIIIaIntrinsic XaseBase-paired stemActive site functionAssembly of prothrombinaseFactor Xa and factor VaSELEX screeningMolecular replacementInteracting proteinsProteinase domainFunctional characterizationAptamer bindingCatalytic Ser195Disrupt interactionsA-resolutionFactor XaHeparin bindingStructural basisAutolysis loopNucleotideInteracting speciesNucleotide basesSolvent accessible surface area
2009
Structural basis for EGFR ligand sequestration by Argos
Klein D, Stayrook S, Shi F, Narayan K, Lemmon M. Structural basis for EGFR ligand sequestration by Argos. The FASEB Journal 2009, 23: 883.7-883.7. DOI: 10.1096/fasebj.23.1_supplement.883.7.Peer-Reviewed Original ResearchEpidermal growth factor receptorHuman urokinase-type plasminogen activator receptorDiverse developmental processesClamp-like structureEGF-like domainGrowth factor ligandsArgos functionMammalian counterpartsLigand sequestrationEGF-like modulesUrokinase-type plasminogen activator receptorEGF domainsEGF ligandGrowth factor receptorEssential regulatorStructural basisDevelopmental processesStructural homologuesEGFR ligandsFactor ligandHuman cancersPlasminogen activator receptorFactor receptorErbB/Inappropriate activation
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 activatorReceptorsSequestrationProteinActivatorLigandsSpitzTGFTherapeuticsDomainStructural 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
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
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