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
2012
Crystal Structure of a Proteolytic Fragment of ADAMTS13 Reveals Alternative Disulfide Pairings in the Cysteine-Rich Domain
Skipwith C, Stayrook S, Rottensteiner H, Scheiflinger F, Zheng X. Crystal Structure of a Proteolytic Fragment of ADAMTS13 Reveals Alternative Disulfide Pairings in the Cysteine-Rich Domain. Blood 2012, 120: 3363. DOI: 10.1182/blood.v120.21.3363.3363.Peer-Reviewed Original ResearchIntermolecular disulfide bondsSpacer domainExosite interactionsProteolytic fragmentsDisulfide bondsNon-catalytic domainStably transfected Chinese hamster ovary cellsCysteine-rich domainChinese hamster ovary cellsDisulfide pairing patternADAMTS13 spacer domainHamster ovary cellsCys-richCrystallization screeningCysteine residuesDiffracting crystalsVon Willebrand factorX-ray diffractionFree cysteine residuesDisulfide bond pairingsDisulfide pairingPairing patternsCA domainOvary cellsResidues
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