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
2007
Prevalence of the EH1 Groucho interaction motif in the metazoan Fox family of transcriptional regulators
Yaklichkin S, Vekker A, Stayrook S, Lewis M, Kessler D. Prevalence of the EH1 Groucho interaction motif in the metazoan Fox family of transcriptional regulators. BMC Genomics 2007, 8: 201. PMID: 17598915, PMCID: PMC1939712, DOI: 10.1186/1471-2164-8-201.Peer-Reviewed Original ResearchConceptsEh1-like motifsFox gene familyFox family proteinsFox proteinsGroucho interaction motifEh1 motifGene familyTranscriptional regulationFOX familyFamily proteinsInteraction motifsStructure predictionWinged helix DNA-binding domainFamily of transcriptional regulatorsSecondary structure predictionDNA-binding domainN-terminal motifSwiss protein databaseManual sequence alignmentFOX family genesDivergent speciesSequence alignmentProtein sequencesProtein databaseTranscriptional corepressor
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